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Showing RANBP2 — NUP358 is a alias.

RANBP2

E3 SUMO-protein ligase RanBP2 · UniProt P49792

Length
3224 aa
Mass
358.2 kDa
Annotated
2026-06-10
100 papers in source corpus 59 papers cited in narrative 59 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RANBP2/Nup358 is a large multidomain nucleoporin anchored to the cytoplasmic filaments of the nuclear pore complex, where it integrates nucleocytoplasmic transport, SUMO conjugation, and cytoskeletal motor regulation (PMID:7775481, PMID:9398662). Its best-defined activity is as a non-RING, non-HECT SUMO E3 ligase: a ~33 kDa internal-repeat region binds the E2 enzyme Ubc9 and positions the SUMO-charged thioester for transfer to substrates (PMID:11792325, PMID:15378033). Structural and reconstitution work established that RANBP2 functions physiologically not as a free protein but as a composite multisubunit ligase quantitatively associated with RanGAP1*SUMO1 and Ubc9, in which complex formation activates a catalytic site absent in free RANBP2 (PMID:15931224, PMID:22464730). Through this activity it sumoylates a defined set of substrates—Topoisomerase IIα, Borealin, HDAC4, SHP, and FTO—controlling inner-centromere targeting and chromosome segregation, chromosomal passenger complex regulation, transcriptional repression, and downstream metabolic and epigenetic outputs (PMID:18394993, PMID:18946085, PMID:12032081, PMID:27412403, PMID:32154934). At the cytoplasmic NPC face the same RANBP2/RanGAP1*SUMO1/Ubc9 complex acts as an autonomous disassembly machine for CRM1 export complexes via tandem FG-repeat patches and Ran-binding domains, and serves as a Ran-GTP-dependent platform that recycles importin-β and supports import via importin-α/β, transportin, and NXF1 pathways; an N-terminal fragment bearing the NPC-anchoring region, FG motifs, and one Ran-binding domain is sufficient to rescue transport and viability (PMID:27160050, PMID:10473610, PMID:21859863, PMID:14729961). Independent of transport, RANBP2 is an allosteric activator of kinesin-1 (KIF5B/KIF5C) through a dedicated kinesin-binding domain and activates dynein/dynactin/BicD2 motility, and its C-terminal cyclophilin domain is a prolyl isomerase and chaperone acting on red/green opsin and HIV-1 capsid (PMID:19305391, PMID:35229716, PMID:8857542, PMID:23902822). Genetic separation in mouse models shows that the cyclophilin PPIase and chaperone/SUMO-binding activities are mechanistically distinct, and that individual Ran-binding domains carry cell-type-specific functions in retinal photoreceptors (PMID:24403063, PMID:25187515).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1995 High

    Establishing the architecture and location of Nup358 defined it as the major cytoplasmic-filament nucleoporin with the domain repertoire that would explain its later multifunctionality.

    Evidence cDNA cloning, immunofluorescence and immunogold EM localizing it to the tips of cytoplasmic NPC fibers

    PMID:7775481

    Open questions at the time
    • Domain functions inferred from sequence, not yet tested biochemically
    • No structures of individual domains at this stage
  2. 1997 High

    Linking SUMO-modified RanGAP1 to RANBP2 docking showed that Ran GTP hydrolysis at the cytoplasmic NPC face is required for nuclear protein import, defining a functional transport role.

    Evidence Immunofluorescence, antibody inhibition of import, biochemical pulldown, and RanGAP activity assays of the RanGAP1*SUMO1/Ubc9/RanBP2 complex

    PMID:9019411 PMID:9108047 PMID:9398662

    Open questions at the time
    • Did not establish RANBP2 as an enzyme itself
    • Mechanism of importin-β capture/release not yet resolved
  3. 2002 High

    Identifying RANBP2 as a SUMO1 E3 ligase distinct from RING/HECT and PIAS families redefined it from a passive scaffold to an enzyme, and identified its first substrates.

    Evidence In vitro SUMOylation assays, domain mapping, and substrate modification of Sp100, HDAC4, and Mdm2

    PMID:11792325 PMID:12032081 PMID:12393906

    Open questions at the time
    • Mdm2 substrate (idx 32) supported by single-lab in vitro reconstitution
    • Whether free RANBP2 is the physiological catalytic species unresolved
  4. 2005 High

    Structural and biochemical dissection explained the catalytic mechanism: RANBP2 binds both Ubc9 and SUMO to orient the E2-thioester, using SUMO-paralog-selective contacts and unstructured catalytic segments unlike canonical E3s.

    Evidence Crystal structure of Ubc9/RanBP2/SUMO1-RanGAP1, NMR chemical shift perturbation, stoichiometry analysis and mutagenesis

    PMID:15378033 PMID:15608651 PMID:15931224 PMID:16194093

    Open questions at the time
    • Built on minimal IR1-M fragment rather than full-length protein
    • AutoSUMOylation sites (idx 40) lacked mutagenesis validation
  5. 2008 High

    Demonstrating that RANBP2 acts as a composite ligase with RanGAP1*SUMO1/Ubc9 resolved the discrepancy between weak free-enzyme activity and cellular substrate specificity, and linked the enzyme to mitotic substrates.

    Evidence Biochemical reconstitution, quantitative proteomics, in vitro SUMOylation of Topo IIα and Borealin, and conditional mouse genetics

    PMID:18394993 PMID:18946085 PMID:22464730

    Open questions at the time
    • How complex assembly is regulated in vivo across the cell cycle not fully defined
    • Opposing SENP3 deconjugation cycle characterized only for Borealin
  6. 2004 High

    Defining RANBP2 as the cytoplasmic site of CRM1 export-complex disassembly and importin-β recycling established its mechanistic role in completing transport cycles.

    Evidence RNAi epistasis, NES-peptide arrest, in vitro binding and GTPase coupling assays, and reconstituted disassembly intermediates

    PMID:10473610 PMID:10601307 PMID:14993277 PMID:15329671 PMID:27160050

    Open questions at the time
    • Relative contributions of FG patches versus Ran-binding domains to disassembly resolved only in vitro
    • CRM1-docking via zinc fingers (idx 20) from single lab
  7. 2011 High

    Conditional knockout and domain-rescue defined which RANBP2 modules are essential for viability and transport, showing a minimal N-terminal fragment suffices for multiple import/export pathways.

    Evidence Conditional knockout MEFs with mutant rescue, transportin- and cargo-specific import assays, and overexpression rescue identifying rate-limiting receptors

    PMID:14729961 PMID:18305100 PMID:19299463 PMID:21859863 PMID:21995724

    Open questions at the time
    • Cargo-specific assembly platform roles (idx 44) from single lab
    • Distinct cargo determinants for receptor selection incompletely mapped
  8. 2009 High

    Identifying the kinesin-binding domain and showing allosteric activation of KIF5B established a transport-independent cytoskeletal motor function for RANBP2.

    Evidence Domain mapping, isotype-selective in vitro binding/mutagenesis, ATPase kinetics, and mitochondrial phenotype assays

    PMID:11553612 PMID:17887960 PMID:19305391

    Open questions at the time
    • In vivo significance of kinesin activation at intact NPCs not directly tested
    • How motor binding is coordinated with NPC anchoring unknown
  9. 2013 High

    High-resolution structures of the N-terminal, cyclophilin, and full C-terminal domains revealed atypical folds—TPR repeats binding ssRNA and a non-canonical cyclophilin active site—rationalizing chaperone/PPIase activity toward opsin and HIV-1 capsid.

    Evidence X-ray crystallography of NTD and CTD, NMR isomerization assays, and RNA-binding/PPIase assays

    PMID:22959972 PMID:23353830 PMID:23902822 PMID:8857542

    Open questions at the time
    • PPIase activity measured as weak in vitro; physiological substrate range beyond opsin/capsid not defined
    • Functional consequence of NTD ssRNA binding unresolved
  10. 2014 High

    In vivo genetic separation of RANBP2 enzymatic activities showed PPIase and chaperone/SUMO-binding functions are distinct and that individual Ran-binding domains have cell-type-specific roles.

    Evidence BAC transgenic mice with point-mutant Ranbp2 (R2944A, CLDm) and domain-selective complementation, with retinal proteostasis and electrophysiology readouts

    PMID:24403063 PMID:25187515 PMID:57

    Open questions at the time
    • Molecular targets linking PPIase activity to hnRNP A2/B1 downregulation not defined
    • Mechanism of cell-type specificity of RBD2/RBD3 requirements unknown
  11. 2016 Medium

    Extending substrate scope to SHP and FTO connected RANBP2 SUMO ligase activity to bile-acid transcriptional control and m6A RNA modification, broadening its physiological output.

    Evidence In vitro SUMOylation, mouse K68R SHP genetics, ChIP, and m6A sequencing

    PMID:27412403 PMID:32154934

    Open questions at the time
    • FTO/SHP pathways each established by single labs
    • Whether composite NPC complex or a soluble pool catalyzes these modifications unclear
  12. 2022 High

    Structural definition of a coil-to-helix transition at the BicD2 interface showed RANBP2 also activates dynein/dynactin motility, complementing its kinesin role in bidirectional transport.

    Evidence NMR titration/CEST, circular dichroism, mutagenesis, and single-molecule motility reconstitution

    PMID:35229716

    Open questions at the time
    • Cellular contexts where RANBP2 activates dynein versus kinesin not resolved
    • Coordination with NPC-anchored pool unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How RANBP2's many separable activities—SUMO ligation, transport-cycle disassembly, motor activation, and PPIase chaperoning—are spatially and temporally partitioned within a single protein remains unresolved.
  • No integrated model coordinating enzymatic versus scaffolding roles
  • Tissue-specific functional partitioning (CNS, retina, muscle, liver) mechanistically unexplained
  • Regulation by phosphorylation and Parkin-mediated turnover only partly characterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 9 GO:0008092 cytoskeletal protein binding 5 GO:0060090 molecular adaptor activity 4 GO:0016853 isomerase activity 3 GO:0044183 protein folding chaperone 3 GO:0098772 molecular function regulator activity 3 GO:0003723 RNA binding 2
Localization
GO:0005635 nuclear envelope 3 GO:0005856 cytoskeleton 2 GO:0005829 cytosol 1
Pathway
R-HSA-9609507 Protein localization 6 R-HSA-1640170 Cell Cycle 5 R-HSA-392499 Metabolism of proteins 5 R-HSA-8953854 Metabolism of RNA 4 R-HSA-1643685 Disease 3
Partners
AGO2BICD2EPAC1KIF5BKPNB1RANGAP1UBE2IXPO1
Complex memberships
RanBP2/RanGAP1*SUMO1/Ubc9 composite SUMO E3 ligasenuclear pore complex cytoplasmic filaments

Evidence

Reading pass · 59 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 SUMO-1 (small ubiquitin-related modifier) conjugation of RanGAP1 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 in a manner that cannot be rescued by soluble cytosolic RanGAP1, indicating that GTP hydrolysis by Ran at RanBP2 is required for nuclear protein import. Immunofluorescence microscopy, antibody inhibition of nuclear import, biochemical pulldown Cell High 9019411
1995 Nup358/RanBP2 localizes to the cytoplasmic fibers of the nuclear pore complex and contains four Ran-GTP binding domains, zinc finger motifs, FG/FXFG repeats, and a cyclophilin A homologous domain; immunogold electron microscopy sublocalized it at the tip of cytoplasmic NPC fibers. Immunofluorescence microscopy, immunogold electron microscopy, cDNA cloning and sequence analysis 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 Sp100. The E3-like activity resides in a 33 kDa domain lacking RING finger motifs, distinct from PIAS family E3 ligases. In vitro SUMOylation assays, co-immunoprecipitation, domain mapping Cell High 11792325
2005 Crystal structure at 3.0 Å of the four-protein complex of Ubc9, RanBP2 E3 ligase domain (IR1-M), and SUMO-1 conjugated to RanGAP1 C-terminal domain reveals that RanBP2 acts as an E3 by binding both SUMO and Ubc9 to position the SUMO-E2-thioester in an optimal orientation for conjugation. X-ray crystallography, biochemical kinetic assays, mutagenesis Nature High 15931224
2004 RanBP2's 30 kDa catalytic fragment is a largely unstructured protein that binds Ubc9 in a 1:1 stoichiometry via hydrophobic interactions at nine RanBP2 and three Ubc9 side chains; two partially overlapping 79-residue catalytic domains within RanBP2 are sufficient for maximal E3 activity, distinguishing RanBP2 from all HECT- and RING-type E3 ligases. Biochemical mutagenesis, stoichiometry analysis, in vitro SUMOylation assays, structural characterization Nature structural & molecular biology High 15378033
2004 NMR chemical shift perturbation identified that RanBP2 binds to the beta-sheet of Ubc9 (unlike canonical ubiquitin E2-E3 interactions). RanBP2 contains a binding site specific for SUMO-1 but not SUMO-2, enabling SUMO paralog-selective conjugation; mutational disruption of Ubc9-RanBP2 binding affected SUMO-2 but not SUMO-1 conjugation to Sp100 and PML. NMR chemical shift perturbation, mutagenesis, in vitro SUMOylation assays Nature structural & molecular biology High 15608651
2012 Cellular RanBP2 is quantitatively associated with RanGAP1*SUMO1/Ubc9, forming a composite multisubunit SUMO E3 ligase complex. Biochemical reconstitution showed the complex has activity on Borealin that is not present in free RanBP2; complex formation induces activation of a catalytic site absent in free RanBP2. Biochemical reconstitution, in vitro SUMOylation assays, co-immunoprecipitation, quantitative proteomics Molecular cell High 22464730
2008 RanBP2 sumoylates Topoisomerase IIα (Topo IIα) during mitosis; this SUMO modification is required for Topo IIα localization to inner centromeres. Mice with low RanBP2 develop aneuploidy with anaphase bridge formation due to failure of Topo IIα to accumulate at inner centromeres, in the absence of overt transport defects. Conditional hypomorphic mouse model, immunofluorescence, in vitro SUMOylation assays, cytogenetic analysis Cell High 18394993
2002 RanBP2 catalyzes SUMO-1 modification of HDAC4 at the nuclear pore complex; HDAC4 sumoylation depends on its ability to self-aggregate and on an intact nuclear localization signal, and is coupled to nuclear import. A sumoylation-deficient HDAC4-K559R mutant shows reduced transcriptional repression and histone deacetylase activity. Co-transfection, mutagenesis, in vitro SUMOylation assays, immunofluorescence The EMBO journal High 12032081
1997 RanBP2 forms a stable complex with modified RanGAP1 (SUMO-conjugated) and Ubc9p (Xenopus homolog of E2 ubiquitin-conjugating enzyme); the complex retains GTPase-activating protein activity, indicating RanGAP1 is not inactivated by SUMO modification. Immunoprecipitation, RanGAP activity assays, cDNA cloning Proceedings of the National Academy of Sciences of the United States of America High 9108047
1998 Ubc9p (Xenopus homolog) acts as an E2-like enzyme for SUMO-1 conjugation but not 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 conjugation assays, co-immunoprecipitation, domain mapping Current biology : CB High 9427648
2004 RanGAP1–RanBP2 complex is required for microtubule-kinetochore interactions in mitosis; RanBP2 depletion causes mislocalization of RanGAP1, Mad1, Mad2, CENP-E, and CENP-F and loss of cold-stable kinetochore-MT interactions. RanGAP1 and RanBP2 are targeted to kinetochores as a single complex dependent on Hec1/Ndc80 and Nuf2 (but not CENP-I, Bub1, or CENP-E). siRNA depletion, immunofluorescence, co-immunoprecipitation, live cell imaging Current biology : CB High 15062103
2003 Nup358/RanBP2 is essential for kinetochore function; siRNA-mediated depletion of Nup358 severely perturbs chromosome congression and segregation and inhibits the assembly of other kinetochore components, leading to aberrant kinetochore structure. siRNA depletion, live cell imaging, immunofluorescence microscopy The Journal of cell biology High 12963708
1997 RanGTP specifically promotes binding of p97 (importin beta) to RanBP2, whereas it inhibits p97 binding to other FG repeat nucleoporins; purified RanBP2 forms a flexible ~36 nm filamentous molecule constituting cytoplasmic fibrils of the NPC. Biochemical purification from rat liver nuclear envelopes, in vitro binding assays, electron microscopy Molecular biology of the cell High 9398662
2004 Nup88 and Nup214/CAN mediate the attachment of Nup358/RanBP2 to the NPC; RNAi of Nup88 or Nup214 causes strong reduction of Nup358 at the nuclear envelope. Nup358 depletion reduces CRM1 localization at the cytoplasmic NPC face and causes a distinct reduction in NES-dependent nuclear export. RNA interference, immunofluorescence, co-immunoprecipitation, nuclear export assays Molecular and cellular biology High 14993277
2004 RanBP2/Nup358 provides a major binding site for NXF1-p15 heterodimers at the cytoplasmic NPC filaments; RanBP2 depletion in Drosophila cells inhibits mRNA export and causes release of NXF1 into the cytoplasm, reducing its nuclear levels, while CRM1-mediated protein export is unaffected. RNAi in Drosophila cells, mRNA export assays, immunofluorescence, in vitro binding assays Molecular and cellular biology High 14729961
1996 The RBD4 and cyclophilin domains of RanBP2 act in concert as a chaperone for red/green opsin: RBD4 binds opsin and the cyclophilin domain augments and stabilizes this interaction, possibly through proline isomerization of the opsin substrate, unlike Drosophila NinaA which forms a stable complex with opsin. In vitro binding assays, domain deletion analysis Nature High 8857542
2001 A novel kinesin-binding domain (KBD) of RanBP2, located between RBD2 and RBD3, associates selectively and directly with kinesin motors KIF5B and KIF5C but not KIF5A in the CNS; kinesin light chain and RanGTPase are also part of this macroassembly complex. In vitro pulldown, co-immunoprecipitation, domain mapping The Journal of biological chemistry High 11553612
2007 The kinesin-binding domain (KBD) of RanBP2 associates selectively and directly with KIF5B and KIF5C via a ~100-residue segment including a leucine-like heptad motif; a single residue conserved in KIF5B/C but not KIF5A confers isotype-specific binding. Selective inhibition of KBD-KIF5B/C interaction causes perinuclear clustering of mitochondria, deficits in mitochondrial membrane potential, and cell shrinkage. In vitro binding assays with purified proteins, mutagenesis, cell-based functional assays, mitochondrial membrane potential measurements Traffic (Copenhagen, Denmark) High 17887960
2009 RanBP2 is the first known allosteric activator of kinesin-1 (KIF5B): the KBD with flanking RBD2/RBD3 domains activates KIF5B ATPase activity ~30-fold in the presence of microtubules and ATP in a biphasic, highly cooperative manner. Deletion of one RBD lowers activation 3-fold and abolishes cooperativity. 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 exportin-1/CRM1 during nuclear export; this interaction is insensitive to leptomycin B and to the nucleotide-bound state of Ran-GTPase, unlike Ran's interaction with the RanBP2-exportin-1 complex. In vitro binding assays, domain mapping, leptomycin B treatment The Journal of biological chemistry Medium 10601307
1999 Karyopherin beta1 (importin beta) binds RanBP1-homologous (RBH) domains of Nup358 in the presence of either RanGTP or RanGDP; a classical NLS peptide bound to the Kapbeta1-RanGTP-RBH complex stimulates GTP hydrolysis by RanGAP1, linking termination of one import cycle with initiation of the next. In vitro binding assays, GTPase activity assays, ultrastructural analysis, permeabilized cell import assays The Journal of biological chemistry High 10473610
2011 RanGTP-importin-β binding to the Ran-binding domain (RBD) of RanBP2 at cytoplasmic fibrils is required for cNLS-mediated protein import and cell viability. Conditional knockout of RanBP2 in MEFs causes cell death with defects in M9- and cNLS-mediated import, NES-mediated export, and mRNA export; an N-terminal RanBP2 fragment with the NPC-binding domain, three FG motifs, and one RBD rescues all transport defects and viability. Conditional knockout mouse embryonic fibroblasts, Cre-mediated inactivation, nuclear transport assays, mutant rescue analysis The Journal of cell biology High 21859863
2008 The Nup358-RanGAP1 complex has a dual function in nuclear import: it coordinates importin beta recycling and reformation of novel import complexes. Depletion of Nup358 reduces importin alpha/beta-dependent nuclear import; overexpression of importin beta rescues import in Nup358-depleted cells, demonstrating importin beta is rate-limiting. RNAi, in vitro transport assays, antibody inhibition, overexpression rescue Molecular biology of the cell High 18305100
2006 RanBP2 associates in vitro and in vivo with the mitochondrial metallochaperone Cox11 and hexokinase type I (HKI) via its leucine-rich domain; the leucine-rich domain has chaperone activity toward Cox11. Cox11 inhibits HKI, and RanBP2 suppresses this inhibitory activity. RanBP2 haploinsufficiency in mice decreases HKI and ATP levels selectively in the CNS. In vitro binding assays, co-immunoprecipitation, enzyme activity assays, mouse genetic model PLoS genetics High 17069463
2008 RanBP2 promotes SUMO2/3 modification of Borealin (a chromosomal passenger complex component) during mitosis; RanBP2 interacts with the CPC and stimulates Borealin SUMOylation in vitro. SENP3 catalyzes deconjugation of SUMO2/3 from Borealin, constituting a mitotic conjugation-deconjugation cycle. Co-immunoprecipitation, in vitro SUMOylation assays, siRNA depletion, cell synchronization Molecular biology of the cell High 18946085
2016 The RanBP2/RanGAP1*SUMO1/Ubc9 complex functions as an autonomous disassembly machine for Crm1 export complexes: three in vitro reconstituted intermediates show binding of Crm1 export complexes via two FG-repeat patches, cargo release by RanBP2's Ran-binding domains, and retention of free Crm1 at RanBP2 after Ran-GTP hydrolysis. In vitro reconstitution of disassembly intermediates, biochemical fractionation, pulldown assays Nature communications High 27160050
2013 The cyclophilin domain of NUP358 is an active prolyl isomerase that catalyzes cis-trans isomerization of the HIV-1 capsid at residue P90; crystal structure of the N-terminal HIV-1 capsid domain complexed with the NUP358 cyclophilin domain shows positioning allowing single-bond resonance stabilization of P90. X-ray crystallography, NMR exchange experiments, in vitro isomerization assays Retrovirology High 23902822
2013 Crystal structure of the C-terminal domain (CTD) of Nup358 at 1.75 Å reveals a cyclophilin-like fold with a non-canonical active-site configuration possessing weak peptidyl-prolyl isomerase activity; the active-site cavity mediates weak association with HIV-1 capsid. The CTD is dispensable for nuclear envelope localization of Nup358. X-ray crystallography, biochemical PPIase assays, localization assays Journal of molecular biology High 23353830
2012 Crystal structure of the Nup358 N-terminal domain (NTD) at 0.95 Å reveals an α-helical domain with three central tetratricopeptide repeats (TPRs) adopting an extended conformation lacking the canonical peptide-binding groove; the NTD possesses positively charged surface and can bind single-stranded RNA. X-ray crystallography, RNA binding assays Journal of molecular biology High 22959972
2011 RanBP2 is required for transportin-mediated nuclear import; Nup358 depletion strongly inhibits nuclear import of HIV-1 Rev and other transportin-dependent cargoes; overexpression of transportin rescues import in Nup358-depleted cells, demonstrating that transportin becomes rate-limiting. siRNA depletion, nuclear import assays, overexpression rescue in HeLa cells Journal of cell science High 19299463
2004 RanGAP1*SUMO1 is phosphorylated at T409, S428, and S442 by cyclin B/Cdk1 before nuclear envelope breakdown and remains associated with RanBP2/Nup358 and Ubc9 throughout mitosis, suggesting mitotic phosphorylation may regulate the RanGTPase cycle and/or RanBP2-dependent SUMOylation. Mass spectrometry, in vitro kinase assay, co-immunoprecipitation, cell synchronization The Journal of cell biology High 15037602
2002 RanBP2 sumoylates Mdm2; in vitro, RanBP2 catalyzes SUMO modification of Mdm2 at the nuclear pore during nuclear translocation. The K182R Mdm2 mutant, which localizes exclusively to the cytoplasm, is not sumoylated in intact cells but can be sumoylated in vitro, consistent with RanBP2 sumoylating Mdm2 during nuclear import. In vitro SUMOylation assays, mutagenesis, co-transfection, immunofluorescence The Journal of biological chemistry Medium 12393906
2011 Nup358/RanBP2 directly interacts with zinc finger repeats to bind ALREX-promoting RNA elements in mRNAs encoding secretory proteins; Nup358 is required for stimulated translation of these mRNAs and for efficient global synthesis of proteins targeted to the ER and mitochondria. RNA binding assays, siRNA depletion, polysome/translation assays PLoS biology Medium 23630457
2011 RanBP2 directly interacts with the zinc fingers (ZNFs) to bind and tether Epac1 (a cAMP-regulated GEF for Rap) to the NPC; RanBP2 inhibits the catalytic CDC25 homology domain of Epac1 in vitro. RanBP2 depletion releases Epac1 from the NPC and enhances cAMP-induced Rap activation and cell adhesion. Phosphorylation of RanBP2 ZNFs also releases Epac1. Co-immunoprecipitation, in vitro GEF activity assay, siRNA depletion, phosphorylation analysis The Journal of cell biology High 21670213
2005 Parkin (E3 ubiquitin ligase) selectively binds RanBP2 and ubiquitinates it, promoting proteasomal degradation of RanBP2. Parkin also controls intracellular levels of sumoylated HDAC4 as a downstream consequence of RanBP2 ubiquitination. Co-immunoprecipitation, in vitro ubiquitination assay, proteasome inhibitor treatment The Journal of biological chemistry Medium 16332688
2005 Depletion of Nup358/RanBP2 by siRNA completely abolishes SUMOylation along the nuclear rim and dislocates RanGAP1 from NPCs; Nup358 depletion also markedly reduces the number of PML bodies, suggesting RanBP2-mediated SUMOylation at the nuclear rim is required for PML body formation. In situ SUMOylation assay in semi-intact cells, siRNA knockdown, immunofluorescence Experimental cell research Medium 16688858
2001 The IR1+2 domain (129 amino acids) of RanBP2 binds Ubc9 with high affinity in vitro and in vivo; overexpression of GFP-IR1+2 sequesters ~90% of nuclear Ubc9 in the cytoplasm, mislocalizes SUMO-1/2/3 and PML, and prevents Rad51 foci formation, indicating a role of nuclear Ubc9 in Rad51-mediated homologous recombination. In vitro binding assays, co-immunoprecipitation, GFP-fusion overexpression, immunofluorescence The Journal of biological chemistry Medium 11709548
2007 A fraction of Nup358 interacts with interphase microtubules through its N-terminal region; overexpression of this microtubule-targeting domain causes increased microtubule bundling and stability, and elevated acetylated microtubule levels. RNAi depletion of Nup358 affects polarized microtubule stabilization during directed cell migration. Co-sedimentation assay, overexpression, immunofluorescence, RNAi, wound-healing assay FEBS letters Medium 18070602
2004 Supraphysiological high-affinity NES peptides bind CRM1 independently of RanGTP and accumulate (arrest) at Nup358 at the cytoplasmic NPC face, providing in vivo evidence that Nup358 is the site of nuclear export complex disassembly. Peptide library screen, in vitro CRM1-binding assays, RNA interference, immunofluorescence The EMBO journal Medium 15329671
2005 Mass spectrometry (FT-ICR with AI-ECD/IRMPD) identified six in vitro SUMOylation sites in RanBP2 during autoSUMOylation, along with branch-point lysines in SUMO-1 and SUMO-2; all but one site conformed to KxE or KpsiK consensus motifs. In vitro SUMOylation assay, Fourier transform ion cyclotron resonance mass spectrometry Analytical chemistry Medium 16194093
2011 Nup358 binds AGO proteins through its SUMO-interacting motif (SIM); Nup358 promotes the association of target mRNA with miRISC. Nup358 depletion disrupts P bodies and impairs the miRNA-mediated gene silencing pathway. Co-immunoprecipitation, siRNA depletion, pulldown with SIM mutants, P body imaging EMBO reports Medium 28039207
2016 RanBP2 mediates SUMO2 modification of the Small Heterodimer Partner (SHP) at K68 upon bile acid signaling; SUMOylated SHP is transported to the nucleus where it interacts with repressive histone modifiers to inhibit bile acid synthetic genes. Mice expressing a SUMO-defective K68R SHP mutant have increased liver bile acid levels and exacerbated cholestatic pathology. In vitro SUMOylation assays, co-localization studies, mouse genetic model with K68R mutant, ChIP, gene expression analysis Nature communications High 27412403
2015 RanGDP (not RanGTP) is the physiological target for the RanBP2/RanGAP1*SUMO1/Ubc9 complex SUMO E3 ligase activity; transport receptors (Crm1, importin β, Transportin, NTF2) inhibit Ran sumoylation. NTF2 prevents sumoylation by reducing RanGDP's affinity for RanBP2's RBDs to undetectable levels (shown by isothermal titration calorimetry). In vitro SUMOylation assay with reconstituted complex, isothermal titration calorimetry, SENP inhibition in semi-permeabilized cells The Journal of biological chemistry High 26251516
2011 Nup358 functions as a cargo- and receptor-specific assembly platform for nuclear import; a short N-terminal Nup358 fragment promotes import of DBC-1, while DMAP-1 requires a larger fragment. Neither RanGAP interaction nor SUMO E3 ligase activity is required for import of these cargoes. siRNA depletion, nuclear import assays, domain deletion constructs, co-immunoprecipitation Traffic (Copenhagen, Denmark) Medium 21995724
2011 β-catenin directly interacts with RanBP2/Nup358 via Armadillo repeats R10-12; knockdown of endogenous Nup358 impedes the rate of nuclear import/export of β-catenin to a greater extent than that of importin-β, and Nup358 interaction is stimulated by phosphorylation at Tyr-654. FRAP, in vitro export assays, proteomics, co-immunoprecipitation, siRNA knockdown The Journal of biological chemistry Medium 22110128
2005 The zinc finger domain of Nup358, but not a zinc finger from an unrelated protein, binds COPI coatomer and dominantly inhibits nuclear envelope breakdown in an in vitro assay. Nup358-specific antibodies impair nuclear disassembly; individual zinc fingers mediate COPI association, with tandem zinc fingers optimal. In vitro nuclear envelope breakdown assay, in vitro COPI binding, antibody inhibition Molecular biology of the cell Medium 16314393
2009 Nup358 interacts with the middle region of APC and cooperates with kinesin-2 to regulate APC localization to the cell cortex through a nuclear-transport-independent mechanism; Nup358 RNAi impairs polarized cell migration in scratch-induced wound healing assays. Co-immunoprecipitation, ectopic expression, RNAi, wound-healing assay, immunofluorescence Journal of cell science Medium 19654215
2014 Importin 7 is the major soluble nuclear transport receptor for hTERT (telomerase protein component); at the NPC, Nup358's zinc finger region is specifically required for nuclear import of hTERT. siRNA depletion of import receptors, nuclear import assays, Nup358 domain-deletion constructs PloS one Medium 24586428
2016 KIF5B induces relocalization of Nup358 from the nuclear pore into the cytoplasm during HIV-1 infection in a capsid-dependent manner; cytoplasmic Nup358 directly associates with viral cores. This interaction requires both the N74D hydrophobic pocket and the cyclophilin A binding loop (P90A) of capsid. KIF5B knockdown prevents nuclear entry of HIV-1 but not N74D or P90A capsid mutants. siRNA depletion, immunofluorescence, co-immunoprecipitation with viral cores, viral infectivity assays PLoS pathogens Medium 27327622
2011 Depletion of Nup358/RanBP2 or Transportin-3 alters HIV-1 integration site selection, reducing integration in gene-dense regions and near gene-associated features; this phenotype is phenocopied by HIV-1 containing MLV gag, implicating Gag-dependent engagement of transport/pore machinery in integration targeting. siRNA depletion, genome-wide integration site mapping, chimeric virus analysis PLoS pathogens Medium 21423673
2018 RanBP2 interacts with GCN5L1 and αTAT1; genetic silencing of RanBP2 reduces α-tubulin acetylation, phenocopying GCN5L1 depletion. RanBP2 possesses a tubulin-binding domain that recruits GCN5L1 to α-tubulin. Co-immunoprecipitation, siRNA depletion, tubulin acetylation assays Journal of cell science Medium 30333138
2021 The RanBP2/RanGAP1-SUMO nucleocytoplasmic transport hub gates β-arrestin2 (β-arr2) nuclear entry via a non-covalent SUMO-interaction motif (SIM) in β-arr2; depletion of RanBP2/RanGAP1-SUMO levels causes defective β-arr2 nuclear entry. Mutation of the SIM inhibits β-arr2 nuclear import and its ability to delocalize Mdm2 from the nucleus, impairing p53 signaling. Co-immunoprecipitation, siRNA depletion, nuclear import assays, mutagenesis, p53 reporter assays Oncogene Medium 33649538
2020 SIRT1 activates RANBP2, which catalyzes SUMO modification of FTO at K216, promoting FTO degradation; FTO SUMOylation by RANBP2 is required for SIRT1-mediated reduction of FTO and consequent increase in m6A modifications on downstream targets including GNAO1 mRNA. Co-immunoprecipitation, in vitro SUMOylation assays, siRNA depletion, m6A sequencing Hepatology (Baltimore, Md.) Medium 32154934
2022 A Nup358 α-helix (residues 2162-2184) undergoes a coil-to-α-helix transition upon binding the dynein adaptor BicD2, forming the core of the Nup358-BicD2 interface; a minimal Nup358 domain activates dynein/dynactin/BicD2 for processive motility on microtubules. Mutations in this region decrease BicD2 interaction, dynein recruitment, and motility. NMR titration, CEST-NMR, circular dichroism, mutagenesis, in vitro single-molecule motility assays eLife High 35229716
2011 Nup358 depletion in myoblasts suppresses myotube formation without affecting cell viability; the amount of Nup358 within individual NPCs increases during muscle differentiation in C2C12 cells, correlating with structural differences in the cytoplasmic NPC surface detected by atomic force microscopy. siRNA depletion, atomic force microscopy, immunofluorescence, Western blot The FEBS journal Medium 21205196
2012 Depletion of RanBP2 induces cytoplasmic intermediates of nuclear speckles containing phosphorylated SR proteins in G1 phase, disrupting a late step in sequential nuclear entry of mitotic interchromatin granule components; this imbalanced distribution of phosphorylated and hypophosphorylated SR proteins affects alternative splicing patterns. siRNA-based phenotypic screen, immunofluorescence, RT-PCR for alternative splicing Molecular biology of the cell Medium 22262462
2014 Conditional ablation of Ranbp2 in RPE cells causes progressive degeneration; genetic complementation analysis showed that selective impairment of RBD2 and RBD3 (Ran-binding domains 2 and 3) binding to Ran-GTP recapitulates RPE degeneration, while rescuing cone photoreceptor degeneration, revealing domain-specific roles of Ranbp2 in different cell types. Conditional knockout mouse model, BAC transgenic complementation with domain-specific mutations, electrophysiology, immunohistochemistry The Journal of biological chemistry High 25187515
2014 Selective loss of PPIase activity (R2944A mutation) in Ranbp2's cyclophilin domain causes selective deficits in M-opsin biogenesis with accumulation and aggregation in cone photoreceptors, and post-transcriptional down-regulation of hnRNP A2/B1 proteins. Separate chaperone-deficient mutations (CLDm) do not show these effects but abolish SUMO-1 and S1 binding. The two activities are mechanistically separable. BAC transgenic mice expressing point-mutant Ranbp2, proteomics, immunofluorescence, electrophysiology The Journal of biological chemistry High 24403063

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 1033 9019411
2002 The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 690 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 425 7775481
2005 Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 418 15931224
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 270 19118815
2008 Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha. Cell 268 18394993
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 244 15062103
2003 Fusion of ALK to the Ran-binding protein 2 (RANBP2) gene in inflammatory myofibroblastic tumor. Genes, chromosomes & cancer 206 12661011
1996 Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin. Nature 186 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 146 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 141 14993277
2020 SIRT1 Regulates N6 -Methyladenosine RNA Modification in Hepatocarcinogenesis by Inducing RANBP2-Dependent FTO SUMOylation. Hepatology (Baltimore, Md.) 132 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 125 15378033
2008 The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import. Molecular biology of the cell 124 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 117 9398662
2007 Association of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function. Traffic (Copenhagen, Denmark) 107 17887960
2013 HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358. Retrovirology 99 23902822
2016 KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection. PLoS pathogens 98 27327622
2008 RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. Molecular biology of the cell 97 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
2006 RanBP2 modulates Cox11 and hexokinase I activities and haploinsufficiency of RanBP2 causes deficits in glucose metabolism. PLoS genetics 93 17069463
2011 Characterization of a family of RanBP2-type zinc fingers that can recognize single-stranded RNA. Journal of molecular biology 92 21256132
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 90 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
2008 An inflammatory myofibroblastic tumor in liver with ALK and RANBP2 gene rearrangement: combination of distinct morphologic, immunohistochemical, and genetic features. Human pathology 80 18701132
2005 Parkin ubiquitinates and promotes the degradation of RanBP2. The Journal of biological chemistry 80 16332688
2011 The nucleoporin Nup358/RanBP2 promotes nuclear import in a cargo- and transport receptor-specific manner. Traffic (Copenhagen, Denmark) 75 21995724
2007 The nucleoporin Nup358 associates with and regulates interphase microtubules. FEBS letters 74 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
1995 Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex. European journal of cell biology 64 8603673
1999 GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358. The Journal of biological chemistry 63 10473610
2021 YTHDF1 Aggravates the Progression of Cervical Cancer Through m6A-Mediated Up-Regulation of RANBP2. Frontiers in oncology 62 33816306
2013 Structural and functional analysis of the C-terminal domain of Nup358/RanBP2. Journal of molecular biology 62 23353830
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 58 25522933
2014 Nuclear translocation of IGF-1R via p150(Glued) and an importin-β/RanBP2-dependent pathway in cancer cells. Oncogene 56 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
2013 RanBP2/Nup358 potentiates the translation of a subset of mRNAs encoding secretory proteins. PLoS biology 54 23630457
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
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
2016 Nup358 binds to AGO proteins through its SUMO-interacting motifs and promotes the association of target mRNA with miRISC. EMBO reports 47 28039207
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
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 42 24113188
2011 Nup358, a nucleoporin, functions as a key determinant of the nuclear pore complex structure remodeling during skeletal myogenesis. The FEBS journal 42 21205196
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
2015 Sumoylation of the GTPase Ran by the RanBP2 SUMO E3 Ligase Complex. The Journal of biological chemistry 38 26251516
2022 Roles of Nucleoporin RanBP2/Nup358 in Acute Necrotizing Encephalopathy Type 1 (ANE1) and Viral Infection. International journal of molecular sciences 34 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
2018 GCN5L1 interacts with αTAT1 and RanBP2 to regulate hepatic α-tubulin acetylation and lysosome trafficking. Journal of cell science 25 30333138
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
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
2014 Familial acute necrotizing encephalopathy due to mutation in the RANBP2 gene. Journal of the neurological sciences 22 25128471
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 RANBP2-ALK fusion combined with monosomy 7 in acute myelomonocytic leukemia. Cancer genetics 21 24613277
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
2023 RANBP2 evolution and human disease. FEBS letters 19 37795679
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

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