Affinage

RANBP2

E3 SUMO-protein ligase RanBP2 · UniProt P49792

Length
3224 aa
Mass
358.2 kDa
Annotated
2026-04-28
100 papers in source corpus 52 papers cited in narrative 52 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RanBP2/Nup358 is a large multidomain nucleoporin of the cytoplasmic filaments of the nuclear pore complex that integrates nucleocytoplasmic transport, SUMO-dependent signaling, mitotic chromosome segregation, and motor-based organelle trafficking. As a composite SUMO E3 ligase — active only when assembled with RanGAP1*SUMO1 and Ubc9 — RanBP2 catalyzes SUMOylation of substrates including RanGAP1, Topoisomerase IIα (directing it to inner centromeres for sister-chromatid resolution), HDAC4, Borealin, SHP, FTO, and CEBPα, using an intrinsically disordered catalytic domain that positions SUMO and Ubc9 for optimal thioester transfer (PMID:11792325, PMID:15931224, PMID:22464730, PMID:18394993). RanBP2's Ran-binding domains and FG repeats capture RanGTP–importin β complexes to drive cNLS, M9/transportin, and CRM1-dependent transport, while also functioning as an autonomous CRM1 export-complex disassembly machine (PMID:9019411, PMID:21859863, PMID:27160050, PMID:19299463). Beyond the NPC, RanBP2 allosterically activates kinesin-1 (KIF5B/KIF5C) via a dedicated kinesin-binding domain, recruits BicD2 to activate dynein–dynactin processivity, engages NXF1 for mRNA export, isomerizes HIV-1 capsid and red/green opsin via its C-terminal cyclophilin domain, and scaffolds interphase microtubule regulation and tubulin acetylation (PMID:19305391, PMID:35229716, PMID:14729961, PMID:23902822, PMID:8857542, PMID:18070602).

Mechanistic history

Synthesis pass · year-by-year structured walk · 20 steps
  1. 1995 High

    Establishing the molecular identity and NPC localization of a cytoplasmic filament nucleoporin answered the question of what constitutes the cytoplasmic Ran-GTP docking site at the pore.

    Evidence cDNA cloning, immunogold EM, and Ran-GTP binding assay identified RanBP2/Nup358 as a 358 kDa multi-domain protein at cytoplasmic NPC fibrils

    PMID:7775481

    Open questions at the time
    • No functional assay for transport at this stage
    • Domain functions not individually tested
    • Stoichiometry at the NPC undetermined
  2. 1996 High

    Demonstrating that the cyclophilin and RBD4 domains act in concert as a chaperone for red/green opsin revealed an unexpected non-transport function for a nucleoporin.

    Evidence Direct binding and in vitro chaperone assays with domain dissection

    PMID:8857542

    Open questions at the time
    • In vivo relevance for opsin biogenesis not shown
    • Isomerase activity not directly measured in this study
    • Generality to other substrates unknown
  3. 1997 High

    Discovering that SUMOylated RanGAP1 is the species that associates with RanBP2 and that this complex is required for nuclear protein import established the first functional link between SUMO modification and nucleocytoplasmic transport.

    Evidence Co-IP, antibody inhibition of import, and Xenopus extract biochemistry

    PMID:9019411 PMID:9108047

    Open questions at the time
    • Whether RanBP2 itself catalyzes SUMOylation was unknown
    • Mechanistic step in import cycle where GTP hydrolysis acts was unresolved
  4. 1997 High

    Showing that RanGTP specifically promotes importin β binding to RanBP2 — opposite to its effect on other FG nucleoporins — defined RanBP2 as the unique cytoplasmic capture site for RanGTP–importin β complexes.

    Evidence Purified rat liver NPC protein binding assays and EM of filamentous RanBP2

    PMID:9398662

    Open questions at the time
    • No kinetic reconstitution of full import cycle
    • How captured complexes are disassembled was unknown
  5. 1999 High

    Reconstituting a trimeric RanGTP–importin β–RanBP2 complex that couples NLS cargo arrival to RanGAP1-stimulated GTP hydrolysis linked the RanBP2 platform to import cycle reinitiation.

    Evidence In vitro binding and GTPase assay with permeabilized cell import reconstitution

    PMID:10473610

    Open questions at the time
    • Export complex disassembly at RanBP2 not yet addressed
    • Contribution of individual RBDs not dissected
  6. 2002 High

    Identifying RanBP2 as a SUMO1 E3 ligase with a novel non-RING, non-HECT catalytic domain resolved whether RanBP2 merely scaffolds or actively catalyzes SUMOylation, and expanded the repertoire of E3 ligase architectures.

    Evidence In vitro SUMOylation reconstitution with domain mapping showing a 33 kDa fragment sufficient for E3 activity toward Sp100 and HDAC4

    PMID:11792325 PMID:12032081

    Open questions at the time
    • Structure of catalytic domain unknown
    • Whether E3 activity requires RanGAP1 in vivo was unresolved
    • SUMO paralog specificity not yet addressed
  7. 2003 High

    Demonstrating that RanBP2 depletion causes chromosome congression and segregation failure established that this nucleoporin has essential mitotic functions beyond interphase transport.

    Evidence siRNA knockdown with live-cell imaging and kinetochore component localization in human cells

    PMID:12963708 PMID:15062103

    Open questions at the time
    • Whether mitotic role is through SUMOylation or transport was unclear
    • Specific mitotic substrates not identified
  8. 2004 High

    Mapping the NPC assembly hierarchy showed that Nup88/Nup214 anchor RanBP2 at the cytoplasmic face, and that RanBP2 in turn recruits CRM1, defining the structural basis for export complex docking and NES-dependent export.

    Evidence RNAi epistasis of Nup88/Nup214/RanBP2 with CRM1 localization and NES export assays; supraphysiological NES accumulation at Nup358

    PMID:14993277 PMID:15329671

    Open questions at the time
    • Full disassembly mechanism not reconstituted
    • Zinc finger CRM1 docking site validated by single lab
  9. 2004 High

    NMR and biochemical studies revealed that RanBP2 binds Ubc9's β-sheet surface through a novel interface and contains a SUMO1-specific binding site, explaining SUMO paralog selectivity of the E3 ligase.

    Evidence NMR chemical shift perturbation, mutagenesis, and paralog-specific in vitro SUMOylation

    PMID:15378033 PMID:15608651

    Open questions at the time
    • Full quaternary structure of the active complex unknown
    • Whether SUMO2/3 conjugation uses the same site in vivo unclear
  10. 2004 High

    Identifying RanBP2 as a docking site for NXF1-p15 and showing that its depletion inhibits mRNA export extended RanBP2's role from protein transport to mRNA metabolism.

    Evidence RNAi in Drosophila and human cells with mRNA export assay and NXF1 localization

    PMID:14729961

    Open questions at the time
    • Direct RNA-binding by RanBP2 not yet demonstrated
    • Whether mRNA export role is separable from NXF1 docking unknown
  11. 2005 High

    The crystal structure of the SUMO–RanGAP1–Ubc9–Nup358 quaternary complex provided the atomic mechanism of E3-catalyzed SUMOylation: RanBP2 simultaneously contacts SUMO and Ubc9 to orient the thioester for transfer.

    Evidence 3.0 Å X-ray crystallography with kinetic validation and mutagenesis

    PMID:15931224

    Open questions at the time
    • How substrate is selected and positioned remained open
    • Dynamics of the catalytic cycle unresolved
  12. 2001 High

    Discovery of a dedicated kinesin-binding domain (KBD) in RanBP2 that selectively binds KIF5B/KIF5C but not KIF5A revealed a direct nucleoporin–motor connection, later shown to affect mitochondrial distribution.

    Evidence In vitro pulldown, reciprocal co-IP, domain mapping; dominant-negative KBD causes mitochondrial clustering and membrane potential loss

    PMID:11553612 PMID:17887960

    Open questions at the time
    • Whether KBD–kinesin interaction functions in NPC positioning or cargo transport was unclear
    • Mechanism of motor activation unknown
  13. 2008 High

    Mouse genetics proved that RanBP2 SUMOylates Topoisomerase IIα in mitosis and that this modification is essential for inner centromere targeting, sister chromatid resolution, and genome stability — identifying a specific mitotic SUMO substrate.

    Evidence Hypomorphic RanBP2 mouse model with in vivo SUMOylation assay, Topo IIα localization, and chromosome segregation analysis

    PMID:18394993

    Open questions at the time
    • Whether Topo IIα is the sole critical mitotic substrate was unknown
    • How RanBP2 recognizes Topo IIα as substrate unclear
  14. 2009 High

    Demonstrating that RanBP2's KBD activates KIF5B ATPase ~30-fold cooperatively established RanBP2 as the first known native allosteric activator of kinesin-1, redefining its role from passive scaffold to active motor regulator.

    Evidence In vitro ATPase assay with purified components and domain deletion analysis

    PMID:19305391

    Open questions at the time
    • Cargo identity for KIF5B–RanBP2 transport not defined
    • In vivo validation of cooperative activation not performed
  15. 2011 High

    Conditional knockout showed that a minimal N-terminal RanBP2 fragment with three FG motifs and one RBD rescues all transport pathways (cNLS, M9, NES, mRNA) and cell viability, mapping the essential transport function to RanGTP–importin β capture.

    Evidence Cre-mediated conditional KO in MEFs with structure-function complementation and RBD mutagenesis

    PMID:21859863

    Open questions at the time
    • SUMO E3 ligase function not rescued by this fragment — separability of transport and SUMO functions unclear
    • Whether remaining domains are essential in vivo in organismal context unknown
  16. 2012 High

    Biochemical reconstitution proved that the physiological SUMO E3 ligase is not free RanBP2 but the composite RanBP2/RanGAP1*SUMO1/Ubc9 complex, which possesses a catalytic site absent in the individual components.

    Evidence Quantitative mass spectrometry of endogenous complex, reconstitution with Borealin as substrate

    PMID:22464730

    Open questions at the time
    • How composite active site forms structurally was not resolved
    • Regulation of complex assembly/disassembly unknown
  17. 2013 High

    Structural and functional work on the cyclophilin domain established it as a bona fide prolyl isomerase that catalyzes cis-trans isomerization of HIV-1 capsid P90, explaining the role of Nup358 in HIV-1 nuclear entry.

    Evidence Crystal structures of free CTD (1.75 Å) and CTD–HIV-1 CA complex; NMR exchange spectroscopy confirming isomerase activity

    PMID:23353830 PMID:23902822

    Open questions at the time
    • Whether isomerase activity is required for opsin chaperoning not tested
    • Mechanism by which isomerization promotes HIV nuclear entry not fully defined
  18. 2013 High

    Demonstrating direct RNA binding by RanBP2 zinc fingers and its role in potentiating translation of secretory-protein mRNAs expanded the gene's function to co-translational regulation at the NPC.

    Evidence Direct RNA–protein binding, RNAi, polysome profiling, metabolic labeling; high-resolution crystal structure of NTD showing ssRNA binding

    PMID:22959972 PMID:23630457

    Open questions at the time
    • Specificity of RNA recognition not fully defined
    • Whether translation effect is direct or via mRNA export kinetics not resolved
  19. 2016 High

    Full reconstitution of CRM1 export-complex disassembly at RanBP2 revealed three sequential intermediates — FG-mediated docking, RBD-driven cargo release, and CRM1 retention — demonstrating RanBP2 is an autonomous disassembly machine compatible with simultaneous SUMO E3 activity.

    Evidence In vitro reconstitution of disassembly intermediates with biochemical assays and EM

    PMID:27160050

    Open questions at the time
    • Kinetics of disassembly in vivo not measured
    • Whether simultaneous SUMOylation of export substrates occurs during disassembly untested
  20. 2022 High

    Identification of a minimal Nup358 helix that undergoes disorder-to-helix transition upon BicD2 binding, activating dynein–dynactin processivity, established RanBP2 as an activating adaptor for minus-end-directed transport.

    Evidence NMR, CEST, circular dichroism, mutagenesis, and in vitro single-molecule motility reconstitution

    PMID:35229716

    Open questions at the time
    • In vivo cargo for RanBP2–BicD2–dynein pathway not identified
    • Whether KIF5B and BicD2 adaptations are coordinated unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the diverse functions of RanBP2 — SUMO E3 ligase activity, transport-complex disassembly, motor activation, RNA binding, and prolyl isomerase activity — are coordinated in space and time, and which functions are essential at the organismal level versus in specific tissues, remains incompletely understood.
  • No full-length structure of RanBP2 or in situ cryo-ET model at subnanometer resolution
  • Tissue-specific essential functions beyond CNS motoneurons not systematically mapped
  • Whether SUMO E3 and transport functions are coupled or independent at a single NPC is unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016874 ligase activity 11 GO:0098772 molecular function regulator activity 3 GO:0003723 RNA binding 2 GO:0008092 cytoskeletal protein binding 2 GO:0016853 isomerase activity 2 GO:0044183 protein folding chaperone 2
Localization
GO:0005635 nuclear envelope 4 GO:0005694 chromosome 2 GO:0005856 cytoskeleton 2
Pathway
R-HSA-392499 Metabolism of proteins 8 R-HSA-9609507 Protein localization 6 R-HSA-1640170 Cell Cycle 3 R-HSA-1852241 Organelle biogenesis and maintenance 2 R-HSA-8953854 Metabolism of RNA 2
Partners
BICD2EPAC1KIF5BKIF5CNXF1RANGAP1UBE2IXPO1
Complex memberships
Nuclear pore complex (cytoplasmic filaments)RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase complex

Evidence

Reading pass · 52 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 SUMOylation of RanGAP1 by SUMO-1 is required for its association with RanBP2 at the cytoplasmic periphery of the nuclear pore complex; antibodies against NPC-associated RanGAP1 inhibit nuclear protein import, and this cannot be rescued by soluble cytosolic RanGAP1, indicating GTP hydrolysis by Ran at RanBP2 is required for nuclear protein import. Co-immunoprecipitation, antibody inhibition of nuclear import, subcellular fractionation, immunofluorescence/immunoelectron microscopy Cell High 9019411
1995 RanBP2/Nup358 is a 358 kDa nucleoporin localized at the tip of the cytoplasmic fibers of the nuclear pore complex; it contains four Ran-GTP binding domains, zinc finger motifs, FG repeat motifs, and a C-terminal cyclophilin A homologous domain, establishing it as a binding site for Ran-GTP at the cytoplasmic NPC face. cDNA cloning, immunofluorescence, immunogold electron microscopy, Ran-GTP binding screen The Journal of biological chemistry High 7775481
2002 RanBP2/Nup358 functions as a SUMO1 E3 ligase: it directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1 transfer from Ubc9 to the substrate Sp100; the E3 activity resides in a 33 kDa domain lacking RING finger motifs, distinct from PIAS family E3 ligases. In vitro SUMOylation assay, co-immunoprecipitation, domain mapping, biochemical reconstitution Cell High 11792325
2005 Crystal structure of the four-protein SUMO-RanGAP1-Ubc9-Nup358(IR1-M) complex at 3.0 Å reveals that RanBP2 acts as an E3 by simultaneously binding SUMO and Ubc9 to optimally orient the SUMO-E2-thioester for conjugation, providing the structural basis for RanBP2 SUMO E3 ligase activity. X-ray crystallography (3.0 Å), biochemical kinetic assays, mutagenesis Nature High 15931224
2008 RanBP2 SUMOylates Topoisomerase IIα in mitosis, and this modification is required for Topo IIα localization to inner centromeres; animals with low RanBP2 show failure of sister centromere resolution, anaphase-bridge formation, and severe aneuploidy in the absence of overt transport defects. Mouse genetic model (hypomorphic RanBP2), in vivo SUMOylation assay, immunofluorescence localization, live-cell imaging Cell High 18394993
2002 RanBP2 promotes SUMOylation of the class II histone deacetylase HDAC4 at the nuclear pore complex; CaMK signaling-induced nuclear export abrogates SUMO-1 modification of HDAC4, and sumoylation of HDAC4 is coupled to its nuclear import at the NPC. In vitro SUMOylation assay, co-transfection, site-directed mutagenesis (K559R), nuclear export assay The EMBO journal High 12032081
1997 RanBP2 associates in a complex with SUMOylated RanGAP1 (p88) and Ubc9 (p18/Xenopus homolog of E2 ubiquitin-conjugating enzyme); modification of RanGAP1 is linked to its association with RanBP2 since unmodified RanGAP1 is not found in RanBP2 immunoprecipitates; the RanBP2-RanGAP1-Ubc9 complex retains RanGAP1 GTPase activating activity. Immunoprecipitation from Xenopus egg extracts, RanGAP activity assay, cDNA cloning Proceedings of the National Academy of Sciences of the United States of America High 9108047
1998 Ubc9 (Xenopus p18) acts as an E2-like enzyme for SUMO-1 conjugation (not for ubiquitin conjugation) and interacts specifically with the internal repeat domain of RanBP2, which is itself a substrate for SUMO-1 conjugation in Xenopus egg extracts. In vitro SUMO conjugation assay, domain mapping, co-immunoprecipitation from Xenopus extracts Current biology : CB High 9427648
2004 The RanGAP1-RanBP2 complex is required for microtubule-kinetochore interactions in vivo: depletion of RanBP2 causes mislocalization of RanGAP1, Mad1, Mad2, CENP-E, and CENP-F, loss of cold-stable kinetochore-MT interactions, and accumulation of cells with multipolar spindles; RanGAP1 and RanBP2 are targeted to kinetochores as a complex in a microtubule attachment-dependent manner. siRNA knockdown, immunofluorescence, live-cell imaging, cold-stable kinetochore-MT assay Current biology : CB High 15062103
1996 Two contiguous domains in RanBP2 (Ran-binding domain 4 and cyclophilin domain) act in concert as a chaperone for red/green opsin; the cyclophilin domain does not bind opsin directly but augments and stabilizes the interaction between opsin and RBD4, likely via a cyclophilin-mediated prolyl isomerization of opsin. Direct binding assay, domain mapping, in vitro chaperone activity assay Nature High 8857542
2004 NMR chemical shift perturbation reveals that RanBP2 binds to the β-sheet surface of Ubc9, distinct from known ubiquitin E2-E3 interactions; RanBP2 contains a SUMO-1-specific binding site (not SUMO-2), enabling SUMO paralog-specific conjugation; Ubc9-RanBP2 binding mutations affect SUMO-2 but not SUMO-1 conjugation to Sp100 and PML. NMR chemical shift perturbation, mutagenesis, in vitro SUMOylation assay Nature structural & molecular biology High 15608651
2004 RanBP2's 30-kDa catalytic fragment is largely unstructured and defines a novel class of E3 ligase (neither RING nor HECT type); it binds Ubc9 in 1:1 stoichiometry through largely hydrophobic interactions involving nine RanBP2 and three Ubc9 side chains, suggesting RanBP2 enhances SUMOylation by altering Ubc9's properties rather than mediating substrate interactions. Biochemical reconstitution, domain mutagenesis, binding stoichiometry analysis, in vitro SUMOylation assay Nature structural & molecular biology High 15378033
2003 siRNA-mediated depletion of Nup358/RanBP2 severely perturbs chromosome congression and segregation and strongly inhibits assembly of other kinetochore components, revealing an essential role for Nup358 in kinetochore function and integrating nuclear envelope breakdown with kinetochore maturation. siRNA knockdown, live-cell imaging, immunofluorescence of kinetochore components The Journal of cell biology High 12963708
2012 Cellular RanBP2 is quantitatively associated with RanGAP1, forming a composite multisubunit SUMO E3 ligase (RanBP2/RanGAP1*SUMO1/Ubc9 complex); biochemical reconstitution showed the complex (not free RanBP2) is the relevant E3 ligase in vivo, and complex formation induces activation of a catalytic site that shows no activity in free RanBP2. Biochemical reconstitution, quantitative mass spectrometry, in vitro SUMOylation assay with endogenous substrate Borealin Molecular cell High 22464730
1997 RanGTP specifically promotes binding of p97 (importin β) to RanBP2, whereas RanGTP inhibits p97 binding to other FG-repeat nucleoporins; purified RanBP2 forms a flexible filamentous molecule (~36 nm), consistent with comprising cytoplasmic fibrils. Protein purification from rat liver nuclear envelopes, in vitro binding assay, electron microscopy Molecular biology of the cell High 9398662
2004 Nup88 and Nup214/CAN mediate attachment of Nup358/RanBP2 to the NPC cytoplasmic face; RNAi of Nup88 or Nup214 strongly reduces Nup358 at the NE without reciprocal effect; Nup358 is required for CRM1 localization at the cytoplasmic NPC face and its depletion reduces NES-dependent nuclear export. RNAi knockdown, immunofluorescence, nuclear export assay Molecular and cellular biology High 14993277
2004 RanBP2/Nup358 provides a major binding site for the mRNA export receptor NXF1-p15 at the cytoplasmic NPC filaments; depletion of RanBP2 from Drosophila cells inhibits cell proliferation and mRNA export, and releases NXF1 into the cytoplasm, reducing its nuclear levels. RNAi depletion, immunofluorescence, mRNA export assay, in vitro binding assay Molecular and cellular biology High 14729961
1999 Karyopherin β1 (importin β) bound to RanBP1-homologous (RBH) domains of Nup358 forms a trimeric complex with RanGTP that resists dissociation by RanBP1 alone; interaction of karyopherin α and NLS peptide with this complex stimulates GTP hydrolysis by RanGAP1, linking GTP hydrolysis at Nup358 to reinitiation of nuclear import. In vitro binding assay, permeabilized cell import assay, RanGAP1 GTP hydrolysis assay The Journal of biological chemistry High 10473610
2001 RanBP2 contains a novel kinesin-binding domain (KBD) located between RBD2 and RBD3 that selectively and directly associates with kinesin motors KIF5B and KIF5C (but not KIF5A) both in vitro and in vivo; kinesin light chain and RanGTPase are part of this RanBP2 macroassembly complex. In vitro pulldown, co-immunoprecipitation, domain mapping The Journal of biological chemistry High 11553612
2007 The kinesin-binding domain (KBD) of RanBP2 selectively associates with KIF5B and KIF5C (not KIF5A) through a ~100-residue segment encompassing part of the coiled-coil and globular tail domain; a single conserved residue in KIF5B/KIF5C confers isotype-specific binding; inhibition of KBD-KIF5B/KIF5C interaction causes perinuclear clustering of mitochondria, deficits in mitochondrial membrane potential, and cell shrinkage. Co-immunoprecipitation, in vitro binding, mutagenesis, dominant-negative inhibition with functional phenotypic readout Traffic (Copenhagen, Denmark) High 17887960
2009 RanBP2's kinesin-binding domain (KBD) flanked by RBD2 and RBD3 activates the ATPase activity of KIF5B approximately 30-fold in the presence of microtubules and ATP in a purified in vitro system; activation is biphasic and cooperative; deletion of one RBD reduces activation threefold and abolishes cooperativity; RanBP2 is the first native positive allosteric activator of kinesin-1. In vitro ATPase assay with purified components, domain deletion analysis EMBO reports High 19305391
1999 The zinc finger cluster domain of RanBP2 constitutes a specific docking site for the nuclear export factor exportin-1 (CRM1); this interaction is insensitive to leptomycin B and to the nucleotide-bound state of Ran, indicating it represents a structural platform for CRM1 during nuclear export. In vitro binding assay, domain mapping with truncation constructs The Journal of biological chemistry Medium 10601307
2008 RanBP2 interacts with the chromosomal passenger complex (CPC) component Borealin, stimulates SUMO2/3 modification of Borealin in vitro, and is required for its modification in vivo; SENP3 is a specific interaction partner of Borealin and catalyzes removal of SUMO2/3, defining a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. Co-immunoprecipitation, in vitro SUMOylation assay, siRNA knockdown Molecular biology of the cell High 18946085
2011 The Nup358-RanGAP1 complex is required for efficient importin α/β-dependent nuclear import; Nup358 depletion by RNAi reduces import of multiple reporter proteins; overexpression of importin β rescues import in Nup358-depleted cells, establishing importin β as rate-limiting; NPC-associated RanGAP1 (but not soluble RanGAP1) is required for full rescue of import. RNAi, in vitro transport assay, antibody inhibition, importin β overexpression rescue Molecular biology of the cell High 18305100
2011 Conditional knockout of RanBP2 in mouse embryonic fibroblasts causes cell death with defects in M9- and cNLS-mediated protein import, NES-mediated export, and mRNA export; a short N-terminal RanBP2 fragment with three FG motifs and one Ran-binding domain (RBD) rescues all transport defects and restores viability; mutation of the RBD abrogates RanGTP-importin β capture and cNLS import. Conditional knockout (Cre-mediated), complementation with mutant constructs, transport assays, co-immunoprecipitation The Journal of cell biology High 21859863
2016 The RanBP2/RanGAP1*SUMO1/Ubc9 complex functions as an autonomous disassembly machine preferring the export receptor Crm1; three reconstituted disassembly intermediates were characterized showing: binding of a Crm1 export complex via two FG-repeat patches, cargo-release by RanBP2's Ran-binding domains, and retention of free Crm1 at RanBP2 after Ran-GTP hydrolysis; all intermediates are compatible with SUMO E3 ligase activity. In vitro reconstitution of disassembly intermediates, biochemical assays, electron microscopy Nature communications High 27160050
2011 RanBP2 negatively regulates Epac1 (a cAMP-regulated GEF for Rap) by tethering it to the NPC via direct interaction between Epac1 and RanBP2 zinc fingers; RanBP2 inhibits Epac1 catalytic activity in vitro by binding its CDC25 homology domain; depletion of RanBP2 releases Epac1 from the NPC and enhances cAMP-induced Rap activation and cell adhesion. Co-immunoprecipitation, in vitro catalytic inhibition assay, RNAi depletion, cell adhesion assay The Journal of cell biology High 21670213
2013 RanBP2/Nup358 potentiates translation of mRNAs encoding secretory proteins; ALREX-promoting RNA elements in these mRNAs interact directly with the zinc finger repeats of RanBP2 on the cytoplasmic NPC face; RanBP2 is required for efficient global synthesis of ER-targeted and mitochondrial proteins. Direct RNA-protein binding assay, RNAi knockdown, polysome profiling, metabolic labeling PLoS biology High 23630457
2004 Supraphysiological NES sequences stably bind CRM1 without requiring RanGTP and accumulate at Nup358 in vivo, providing evidence for a nuclear export reaction intermediate where Nup358 is the site of export complex disassembly. Peptide library screen, in vitro binding assay, RNAi, subcellular localization by fluorescence microscopy The EMBO journal Medium 15329671
2009 Depletion of Nup358 strongly inhibits nuclear import of HIV-1 Rev protein; transportin is the major nuclear import receptor for HIV-1 Rev in HeLa cells; overexpression of transportin rescues import in Nup358-depleted cells; Nup358 has a general role in transportin-mediated nuclear import of multiple cargoes. siRNA knockdown, nuclear import assay, receptor overexpression rescue Journal of cell science High 19299463
2013 Crystal structure of the NUP358 cyclophilin domain (CTD) at 1.75 Å reveals a cyclophilin-like fold with non-canonical active-site configuration; the CTD possesses weak peptidyl-prolyl isomerase activity and its active-site cavity mediates weak association with HIV-1 capsid protein; the CTD is dispensable for nuclear envelope localization of Nup358. X-ray crystallography (1.75 Å), PPIase activity assay, capsid binding assay, localization analysis Journal of molecular biology High 23353830
2013 Crystal structure of the Nup358 N-terminal domain at 0.95 Å reveals an α-helical domain with three central TPR motifs in an unusual extended conformation lacking canonical peptide-binding groove; the NTD surface has a conserved positive electrostatic potential and the NTD can bind single-stranded RNA in solution. X-ray crystallography (0.95 Å), RNA binding assay in solution Journal of molecular biology High 22959972
2013 HIV-1 capsid undergoes cis-trans isomerization by the cyclophilin domain of NUP358; crystal structure of HIV-1 N-terminal capsid domain in complex with NUP358 cyclophilin domain shows stabilization of capsid residue P90; NMR exchange experiments confirm NUP358 is an active isomerase for HIV-1 capsid; FIV capsid can bind but is not isomerized by NUP358 and does not require it for infection. X-ray crystallography, NMR exchange spectroscopy, infectivity assay Retrovirology High 23902822
2011 HIV-1 infection induces KIF5B-dependent relocalization of Nup358 into the cytoplasm; cytoplasmic Nup358 directly associates with viral cores in a capsid-dependent manner (requiring both the N74D hydrophobic pocket and P90A cyclophilin loop); KIF5B knockdown prevents nuclear entry and infection by WT but not N74D or P90A capsid mutants; cytoplasmic Nup358 relocalization depends on CPSF6 but not CypA. siRNA knockdown, immunofluorescence, co-immunoprecipitation with viral cores, infectivity assay PLoS pathogens High 27327622
2011 Nup358 interacts with AGO and GW182 proteins via its SUMO-interacting motif (SIM) and promotes the association of target mRNA with miRISC; Nup358 depletion disrupts processing bodies and impairs the miRNA pathway; the SIM is sufficient for direct Nup358-AGO binding. Co-immunoprecipitation, siRNA knockdown, P-body assay, mRNA-miRISC association assay EMBO reports Medium 28039207
2004 Phosphorylation of RanGAP1 on T409, S428, and S442 occurs before nuclear envelope breakdown and is maintained throughout mitosis; cyclin B/Cdk1 phosphorylates RanGAP1 in vitro; phosphorylated RanGAP1 remains associated with RanBP2/Nup358 and Ubc9 in mitosis, suggesting mitotic phosphorylation has functional consequences for the RanGTPase cycle and/or RanBP2-dependent sumoylation. Mass spectrometry (site identification), in vitro kinase assay, co-immunoprecipitation, nocodazole arrest The Journal of cell biology High 15037602
2006 RanBP2 associates in vitro and in vivo with mitochondrial metallochaperone Cox11 and hexokinase I (HKI) via its leucine-rich domain; the leucine-rich domain exhibits chaperone activity toward Cox11; Cox11 strongly inhibits HKI activity and RanBP2 suppresses this inhibitory activity; haploinsufficiency of RanBP2 in mice causes decreased HKI and ATP levels selectively in the CNS and deficits in glucose catabolism. Co-immunoprecipitation, in vitro chaperone assay, HKI activity assay, mouse genetic model PLoS genetics High 17069463
2002 Parkin (ubiquitin E3 ligase) selectively binds to RanBP2 and ubiquitinates it, leading to proteasomal degradation of RanBP2; Parkin-mediated degradation of RanBP2 consequently controls intracellular levels of sumoylated HDAC4. Co-immunoprecipitation, in vitro ubiquitination assay, proteasome inhibitor treatment, immunofluorescence The Journal of biological chemistry Medium 16332688
2015 RanGDP (not RanGTP) is the physiological target for the RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase complex; transport receptors (Crm1, importin β, Transportin, NTF2) all inhibit Ran sumoylation; NTF2 prevents sumoylation by reducing RanGDP affinity for RanBP2's RBDs (measured by ITC); acceptor lysines are accessible in Ran/NTF2 complexes, but binding is abolished. In vitro SUMOylation assay, isothermal titration calorimetry, semi-permeabilized cell assay, site mapping The Journal of biological chemistry High 26251516
2011 Determinants in both IR1 and IR2 of RanBP2's internal repeat domain exhibit specificity for SUMO1 over SUMO2; IR1 is the primary E3 ligase domain and protects RanGAP1-SUMO1/Ubc9; crystal structures of complexes containing UBC9 with RanGAP1-SUMO1/2 show more extensive contacts in SUMO1 complexes, providing the structural basis for SUMO1 specificity. X-ray crystallography, protease protection assay, domain swap constructs, automodification assay The Journal of biological chemistry High 22194619
2007 A fraction of endogenous Nup358 interacts with interphase microtubules through its N-terminal region; overexpression of this microtubule-targeting domain causes increased microtubule bundling, stability, and acetylation; RNAi depletion of Nup358 affects polarized microtubule stabilization during directed cell migration. Co-sedimentation with microtubules, overexpression, RNAi, wound-healing assay, nocodazole resistance assay FEBS letters Medium 18070602
2009 Nup358 interacts with APC through the middle region of APC; ectopic expression of the APC middle region recruits endogenous Nup358 to microtubule plus-ends; Nup358 cooperates with kinesin-2 to regulate APC localization to the cell cortex independent of nuclear transport; RNAi of Nup358 impairs polarized cell migration in a scratch-wound assay. Co-immunoprecipitation, ectopic expression localization, RNAi, wound-healing migration assay Journal of cell science Medium 19654215
2016 RanBP2 co-localizes with SHP at the nuclear envelope upon bile acid signaling and mediates SUMO2 modification of SHP at K68; this SUMOylation facilitates nuclear transport of SHP and its interaction with repressive histone modifiers to inhibit bile acid synthetic genes; mice with SUMO-defective SHP K68R show increased liver bile acid levels and exacerbated cholestatic pathology. Co-immunoprecipitation, in vitro SUMOylation, site-directed mutagenesis (K68R), mouse genetic model, ChIP assay Nature communications High 27412403
2021 The RanBP2/RanGAP1-SUMO complex gates β-arrestin2 (β-arr2) nuclear entry; β-arr2 uses a SIM to interact non-covalently with SUMO at the NPC-associated RanBP2/RanGAP1-SUMO hub; RanBP2 depletion causes defective β-arr2 nuclear import; mutation of the SIM inhibits β-arr2 nuclear import and its ability to delocalize Mdm2 from the nucleus, impairing p53 signaling. Co-immunoprecipitation, RNAi depletion, nuclear import assay, SIM mutagenesis, Mdm2 localization assay, p53 reporter assay Oncogene Medium 33649538
2022 A minimal Nup358 domain (residues 2162-2184) undergoes coil-to-α-helix transition upon binding BicD2, forming the core of the Nup358-BicD2 interface; this interaction activates dynein/dynactin/BicD2 for processive motility on microtubules; mutations in this Nup358 region decrease BicD2 binding, reduce dynein recruitment, and impair motility. NMR titration, CEST, circular dichroism, mutagenesis, in vitro motility reconstitution eLife High 35229716
2005 FT-ICR mass spectrometry identified six sites of in vitro SUMOylation in RanBP2 itself during the RanBP2-catalyzed autoSUMOylation reaction, and four branch-point lysines in SUMO-1 and three in SUMO-2; SUMOylation occurred predominantly at KxE or KψK sequences. FT-ICR mass spectrometry with AI-ECD and IRMPD fragmentation Analytical chemistry Medium 16194093
2020 SIRT1 activates RANBP2 E3 ligase activity, and RANBP2 mediates SUMOylation of the m6A demethylase FTO at K216, promoting its degradation; this mechanism reduces m6A demethylation and downregulates GNAO1 mRNA in hepatocellular carcinoma. Co-immunoprecipitation, SUMOylation assay, site-directed mutagenesis (K216), RNAi, m6A quantification Hepatology (Baltimore, Md.) Medium 32154934
2018 RanBP2 interacts with αTAT1 (α-tubulin acetyltransferase) and GCN5L1; RanBP2 possesses a tubulin-binding domain that recruits GCN5L1 to α-tubulin; siRNA knockdown of RanBP2 reduces α-tubulin acetylation, phenocopying GCN5L1 depletion; this regulatory complex controls lysosome trafficking and positioning. Co-immunoprecipitation, siRNA knockdown, α-tubulin acetylation assay, lysosome localization assay Journal of cell science Medium 30333138
2017 Conditional ablation of Ranbp2 in Thy1+ motoneurons disrupts nucleocytoplasmic partitioning of importin β, exportin 1, Ran GTPase, and HDAC4; causes dysregulation of chemokine receptor Cxcr4/Cxcl12/Cxcl14/Stat3 signaling and proteostasis of hnRNPH3 and metalloproteinase 28; and results in ALS-like syndromes with hindlimb paralysis and motoneuron hypertrophy. Conditional knockout (Cre-mediated), transcriptome analysis, proteomics, immunofluorescence, nerve conduction velocity Disease models & mechanisms High 28100513
2012 Depletion of RanBP2 by RNAi causes G2/M arrest, metaphase catastrophe, and mitotic cell death; RanBP2 N-terminus interacts with importin β1 N-terminus; RanGTPase regulates the RanBP2-importin β1 interaction; a portion of RanBP2 localizes at centrosomes during mitosis. siRNA knockdown, co-immunoprecipitation, flow cytometry, immunofluorescence Cell death & disease Medium 24113188
2005 Nup358 zinc finger domain binds COPI coatomer and dominantly inhibits nuclear envelope breakdown in an in vitro NEBD assay; antibodies against Nup358 impair nuclear disassembly; Nup358 and Nup153 play non-redundant roles in COPI recruitment to the nuclear pore for nuclear envelope breakdown. In vitro nuclear envelope breakdown assay, dominant-negative overexpression, antibody inhibition, co-immunoprecipitation Molecular biology of the cell Medium 16314393
2021 RANBP2 directly interacts with CEBPα transcription factor and facilitates its SUMOylation and degradation; loss of CEBPα reduces OGA transcription, causing global hyper-O-GlcNAcylation in hepatocellular carcinoma cells, including O-GlcNAcylation of PGC1α. Co-immunoprecipitation, in vitro SUMOylation assay, transcription reporter assay, RNAi knockdown, xenograft Cancers Medium 34298689

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1997 A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 1031 9019411
2002 The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 687 11792325
1995 Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. The Journal of biological chemistry 424 7775481
2005 Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 416 15931224
2008 Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha. Cell 267 18394993
2009 Infection-triggered familial or recurrent cases of acute necrotizing encephalopathy caused by mutations in a component of the nuclear pore, RANBP2. American journal of human genetics 266 19118815
2002 The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. The EMBO journal 266 12032081
2004 The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Current biology : CB 241 15062103
2003 Fusion of ALK to the Ran-binding protein 2 (RANBP2) gene in inflammatory myofibroblastic tumor. Genes, chromosomes & cancer 205 12661011
1996 Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin. Nature 185 8857542
2011 HIV integration targeting: a pathway involving Transportin-3 and the nuclear pore protein RanBP2. PLoS pathogens 177 21423673
1997 RanBP2 associates with Ubc9p and a modified form of RanGAP1. Proceedings of the National Academy of Sciences of the United States of America 170 9108047
1998 Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2. Current biology : CB 167 9427648
2003 Nup358 integrates nuclear envelope breakdown with kinetochore assembly. The Journal of cell biology 165 12963708
2000 Live fluorescence imaging reveals early recruitment of emerin, LBR, RanBP2, and Nup153 to reforming functional nuclear envelopes. Journal of cell science 160 10671368
2012 The RanBP2/RanGAP1*SUMO1/Ubc9 complex is a multisubunit SUMO E3 ligase. Molecular cell 144 22464730
2004 Nup358/RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1-mediated nuclear protein export. Molecular and cellular biology 140 14993277
2020 SIRT1 Regulates N6 -Methyladenosine RNA Modification in Hepatocarcinogenesis by Inducing RANBP2-Dependent FTO SUMOylation. Hepatology (Baltimore, Md.) 130 32154934
2004 Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nature structural & molecular biology 128 15608651
2004 The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type. Nature structural & molecular biology 124 15378033
2008 The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import. Molecular biology of the cell 123 18305100
1997 RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex. Molecular biology of the cell 116 9398662
2007 Association of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function. Traffic (Copenhagen, Denmark) 106 17887960
2016 KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection. PLoS pathogens 98 27327622
2013 HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358. Retrovirology 98 23902822
2008 RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. Molecular biology of the cell 96 18946085
2011 Ran-dependent docking of importin-beta to RanBP2/Nup358 filaments is essential for protein import and cell viability. The Journal of cell biology 94 21859863
2011 Characterization of a family of RanBP2-type zinc fingers that can recognize single-stranded RNA. Journal of molecular biology 91 21256132
2006 RanBP2 modulates Cox11 and hexokinase I activities and haploinsufficiency of RanBP2 causes deficits in glucose metabolism. PLoS genetics 91 17069463
2004 RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the nuclear pore complex and functions in nuclear mRNA export. Molecular and cellular biology 88 14729961
2010 Perturbation of host nuclear membrane component RanBP2 impairs the nuclear import of human immunodeficiency virus -1 preintegration complex (DNA). PloS one 87 21179483
2004 Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358. The EMBO journal 87 15329671
2001 The docking of kinesins, KIF5B and KIF5C, to Ran-binding protein 2 (RanBP2) is mediated via a novel RanBP2 domain. The Journal of biological chemistry 87 11553612
2002 Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes. The Journal of biological chemistry 85 12393906
1999 The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1. The Journal of biological chemistry 84 10601307
2016 The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexes. Nature communications 83 27160050
2009 The nuclear pore component Nup358 promotes transportin-dependent nuclear import. Journal of cell science 80 19299463
2005 Parkin ubiquitinates and promotes the degradation of RanBP2. The Journal of biological chemistry 80 16332688
2008 An inflammatory myofibroblastic tumor in liver with ALK and RANBP2 gene rearrangement: combination of distinct morphologic, immunohistochemical, and genetic features. Human pathology 79 18701132
2011 The nucleoporin Nup358/RanBP2 promotes nuclear import in a cargo- and transport receptor-specific manner. Traffic (Copenhagen, Denmark) 73 21995724
2007 The nucleoporin Nup358 associates with and regulates interphase microtubules. FEBS letters 71 18070602
2020 Genetic Acute Necrotizing Encephalopathy Associated with RANBP2: Clinical and Therapeutic Implications in Pediatrics. Multiple sclerosis and related disorders 68 32426208
2011 Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2. The Journal of biological chemistry 67 22194619
2011 Specific armadillo repeat sequences facilitate β-catenin nuclear transport in live cells via direct binding to nucleoporins Nup62, Nup153, and RanBP2/Nup358. The Journal of biological chemistry 65 22110128
1999 GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358. The Journal of biological chemistry 63 10473610
1995 Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex. European journal of cell biology 63 8603673
2013 Structural and functional analysis of the C-terminal domain of Nup358/RanBP2. Journal of molecular biology 62 23353830
2021 YTHDF1 Aggravates the Progression of Cervical Cancer Through m6A-Mediated Up-Regulation of RANBP2. Frontiers in oncology 61 33816306
2014 RANBP2 mutation and acute necrotizing encephalopathy: 2 cases and a literature review of the expanding clinico-radiological phenotype. European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society 57 25522933
2014 Nuclear translocation of IGF-1R via p150(Glued) and an importin-β/RanBP2-dependent pathway in cancer cells. Oncogene 55 24909165
2007 RANBP2 and CLTC are involved in ALK rearrangements in inflammatory myofibroblastic tumors. Cancer genetics and cytogenetics 55 17656252
2000 Different structural and kinetic requirements for the interaction of Ran with the Ran-binding domains from RanBP2 and importin-beta. Biochemistry 55 10995230
2004 RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly. The Journal of cell biology 54 15037602
2014 A case report of epithelioid inflammatory myofibroblastic sarcoma with RANBP2-ALK fusion gene treated with the ALK inhibitor, crizotinib. Japanese journal of clinical oncology 51 25028698
2013 RanBP2/Nup358 potentiates the translation of a subset of mRNAs encoding secretory proteins. PLoS biology 51 23630457
2009 RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system. EMBO reports 51 19305391
2006 In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Experimental cell research 51 16688858
2013 Inflammatory myofibroblastic tumor with RANBP2 and ALK gene rearrangement: a report of two cases and literature review. Diagnostic pathology 50 24034896
2002 Identification of RanBP2- and kinesin-mediated transport pathways with restricted neuronal and subcellular localization. Traffic (Copenhagen, Denmark) 49 12191015
2005 Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction. Analytical chemistry 48 16194093
2008 HDAC-class II specific inhibition involves HDAC proteasome-dependent degradation mediated by RANBP2. Biochimica et biophysica acta 47 18691615
2001 Perturbation of SUMOlation enzyme Ubc9 by distinct domain within nucleoporin RanBP2/Nup358. The Journal of biological chemistry 46 11709548
2016 Nup358 binds to AGO proteins through its SUMO-interacting motifs and promotes the association of target mRNA with miRISC. EMBO reports 45 28039207
2014 A cyclophilin homology domain-independent role for Nup358 in HIV-1 infection. PLoS pathogens 44 24586169
2009 SAGE analysis highlights the importance of p53csv, ddx5, mapkapk2 and ranbp2 to multiple myeloma tumorigenesis. Cancer letters 44 19171422
2017 Loss of Ranbp2 in motoneurons causes disruption of nucleocytoplasmic and chemokine signaling, proteostasis of hnRNPH3 and Mmp28, and development of amyotrophic lateral sclerosis-like syndromes. Disease models & mechanisms 43 28100513
2013 Down-modulation of nucleoporin RanBP2/Nup358 impaired chromosomal alignment and induced mitotic catastrophe. Cell death & disease 41 24113188
2011 The nucleoporin RanBP2 tethers the cAMP effector Epac1 and inhibits its catalytic activity. The Journal of cell biology 41 21670213
2005 Nuclear envelope breakdown is coordinated by both Nup358/RanBP2 and Nup153, two nucleoporins with zinc finger modules. Molecular biology of the cell 41 16314393
2016 Critical role of RanBP2-mediated SUMOylation of Small Heterodimer Partner in maintaining bile acid homeostasis. Nature communications 40 27412403
2011 Nup358, a nucleoporin, functions as a key determinant of the nuclear pore complex structure remodeling during skeletal myogenesis. The FEBS journal 40 21205196
2015 Sumoylation of the GTPase Ran by the RanBP2 SUMO E3 Ligase Complex. The Journal of biological chemistry 36 26251516
2022 Roles of Nucleoporin RanBP2/Nup358 in Acute Necrotizing Encephalopathy Type 1 (ANE1) and Viral Infection. International journal of molecular sciences 32 35408907
2016 Variable clinical course in acute necrotizing encephalopathy and identification of a novel RANBP2 mutation. Brain & development 31 26923722
2012 The distribution of phosphorylated SR proteins and alternative splicing are regulated by RANBP2. Molecular biology of the cell 31 22262462
2012 Crystal structure of the N-terminal domain of Nup358/RanBP2. Journal of molecular biology 31 22959972
2013 Distinct and atypical intrinsic and extrinsic cell death pathways between photoreceptor cell types upon specific ablation of Ranbp2 in cone photoreceptors. PLoS genetics 30 23818861
2012 Ranbp2 haploinsufficiency mediates distinct cellular and biochemical phenotypes in brain and retinal dopaminergic and glia cells elicited by the Parkinsonian neurotoxin, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Cellular and molecular life sciences : CMLS 29 22821000
2009 Nup358 interacts with APC and plays a role in cell polarization. Journal of cell science 28 19654215
2008 Haploinsufficiency of RanBP2 is neuroprotective against light-elicited and age-dependent degeneration of photoreceptor neurons. Cell death and differentiation 27 18949001
2014 Importin 7 and Nup358 promote nuclear import of the protein component of human telomerase. PloS one 25 24586428
2014 Selective impairment of a subset of Ran-GTP-binding domains of ran-binding protein 2 (Ranbp2) suffices to recapitulate the degeneration of the retinal pigment epithelium (RPE) triggered by Ranbp2 ablation. The Journal of biological chemistry 24 25187515
2013 Acute necrotizing encephalopathy (ANE1): rare autosomal-dominant disorder presenting as acute transverse myelitis. Journal of neurology 24 23329376
2020 MxB impedes the NUP358-mediated HIV-1 pre-integration complex nuclear import and viral replication cooperatively with CPSF6. Retrovirology 23 32600399
2020 CD30 and ALK combination therapy has high therapeutic potency in RANBP2-ALK-rearranged epithelioid inflammatory myofibroblastic sarcoma. British journal of cancer 23 32684628
2018 RAN/RANBP2 polymorphisms and neuroblastoma risk in Chinese children: a three-center case-control study. Aging 23 29706609
2018 GCN5L1 interacts with αTAT1 and RanBP2 to regulate hepatic α-tubulin acetylation and lysosome trafficking. Journal of cell science 23 30333138
2011 Immunomodulatory therapy in recurrent acute necrotizing encephalopathy ANE1: is it useful? Brain & development 23 21945312
2022 Coil-to-α-helix transition at the Nup358-BicD2 interface activates BicD2 for dynein recruitment. eLife 22 35229716
2019 Microglial activation in an amyotrophic lateral sclerosis-like model caused by Ranbp2 loss and nucleocytoplasmic transport impairment in retinal ganglion neurons. Cellular and molecular life sciences : CMLS 22 30944974
2016 Nucleoporin Nup358 facilitates nuclear import of Methoprene-tolerant (Met) in an importin β- and Hsp83-dependent manner. Insect biochemistry and molecular biology 22 27979731
2013 inv(2)(p23q13)/RAN-binding protein 2 (RANBP2)-ALK fusion gene in myeloid leukemia that developed in an elderly woman. International journal of hematology 22 24307515
2002 A new clue at the nuclear pore: RanBP2 is an E3 enzyme for SUMO1. Developmental cell 22 11832237
2014 Familial acute necrotizing encephalopathy due to mutation in the RANBP2 gene. Journal of the neurological sciences 21 25128471
2010 Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress. Disease models & mechanisms 21 20682751
2007 Mst1, RanBP2 and eIF4G are new markers for in vivo PI3K activation in murine and human prostate. Carcinogenesis 21 17372272
2021 The RanBP2/RanGAP1-SUMO complex gates β-arrestin2 nuclear entry to regulate the Mdm2-p53 signaling axis. Oncogene 20 33649538
2014 RANBP2-ALK fusion combined with monosomy 7 in acute myelomonocytic leukemia. Cancer genetics 20 24613277
2021 RANBP2 Activates O-GlcNAcylation through Inducing CEBPα-Dependent OGA Downregulation to Promote Hepatocellular Carcinoma Malignant Phenotypes. Cancers 19 34298689
2014 Differential loss of prolyl isomerase or chaperone activity of Ran-binding protein 2 (Ranbp2) unveils distinct physiological roles of its cyclophilin domain in proteostasis. The Journal of biological chemistry 19 24403063