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Showing RABEP1 — RABAPTIN-5 is a alias.

RABEP1

Rab GTPase-binding effector protein 1 · UniProt Q15276

Length
862 aa
Mass
99.3 kDa
Annotated
2026-06-10
39 papers in source corpus 28 papers cited in narrative 27 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RABEP1 (Rabaptin-5) is a coiled-coil endosomal effector that coordinates Rab GTPase signaling to drive early endosome docking, fusion, and receptor recycling (PMID:8521472). It functions as a divalent Rab linker: a 73-residue C-terminal region is necessary and sufficient for binding GTP-Rab5 and Rab5-dependent recruitment to early endosomes, while an N-terminal domain binds GTP-Rab4, and native cytosolic protein exists as a coiled-coil-dependent homodimer (PMID:9524117). Rabaptin-5 forms a tight complex with the Rab5 GEF Rabex-5, increasing its nucleotide exchange activity on Rab5, so that Rab5-GTP recruitment of the Rabaptin-5/Rabex-5 complex generates a positive feedback loop that amplifies Rab5 activation on endosomal membranes (PMID:9323142, PMID:11452015, PMID:20169068). Through defined motifs—including the FGPLV sequence and C-terminal coiled-coils—it links to clathrin adaptors at the TGN/recycling endosomes, binding the gamma1-adaptin ear of AP-1 and the GAE and GAT domains of GGAs, and the complex negatively regulates Rab4-dependent AP-1/clathrin vesicle formation from endosomes (PMID:11872161, PMID:12505986, PMID:14636058, PMID:15331762). PKD phosphorylation at Ser407 redirects Rabaptin-5 to preferentially engage Rab4, driving short-loop recycling of αvβ3 integrin to the leading edge and promoting persistent cell migration and invasion (PMID:22975325); the same recycling activity supports neutrophil motility, where loss of RABEP1 impairs endosomal recycling, Rac/PAK activation, and leading-edge F-actin without affecting bulk Rab5-GTP (PMID:41701563, PMID:40463167). Rabaptin-5 also stabilizes surface levels of receptors such as FcεRI, β1 integrin, and the KV10.1 channel via its recycling function (PMID:18698003, PMID:22841712). During apoptosis, caspase cleavage separates its N- and C-terminal Rab5-binding sites, inactivating endosome fusion (PMID:9321397, PMID:16861912). Activity is further controlled by binding partners HD-PTP/PTPN23, which restrains Rab5 hyperactivation to coordinate ESCRT-dependent MVB sorting (PMID:34657963), and ITSN2L, which promotes RABEP1 degradation (PMID:26633357).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1995 High

    Established RABEP1 as a bona fide Rab5 effector required for endosome fusion, defining its core place in the endocytic pathway.

    Evidence Co-IP, cytosol immunodepletion, and in vitro fusion assay with purified early endosomes plus GTP-dependent recruitment

    PMID:8521472

    Open questions at the time
    • Domain basis of Rab5 binding not yet mapped
    • Did not address other Rab partners or membrane recruitment mechanism
  2. 1997 High

    Identified the Rabaptin-5/Rabex-5 complex, coupling the effector to a Rab5 GEF and explaining how active Rab5 is generated and stabilized at fusion sites.

    Evidence Mass spec identification, biochemical co-purification, in vitro nucleotide exchange and cell-free fusion assays

    PMID:9323142

    Open questions at the time
    • Directionality of regulation (does Rabaptin-5 activate Rabex-5?) not yet resolved
    • Stoichiometry of complex unaddressed
  3. 1997 High

    Showed that caspase cleavage of Rabaptin-5 mechanistically links apoptosis to shutdown of endosome fusion.

    Evidence Cell-free Xenopus apoptosis extract, cleavage immunoblot, caspase inhibitor and Bcl-2/Bcl-xL rescue, fusion assay

    PMID:9321397

    Open questions at the time
    • Exact cleavage sites and responsible caspase not pinpointed
    • Functional consequence of cleavage on domain separation shown only later
  4. 1998 High

    Defined Rabaptin-5 as a divalent Rab linker with separate Rab4 (N-terminal) and Rab5 (C-terminal) binding domains, and as a coiled-coil homodimer.

    Evidence Deletion mutagenesis, GST pulldown, yeast two-hybrid, immunofluorescence, gel filtration

    PMID:9524117

    Open questions at the time
    • Functional consequence of simultaneously bridging Rab4 and Rab5 not demonstrated in vivo
    • Regulation of Rab4 vs Rab5 binding switch unknown at this stage
  5. 2001 High

    Demonstrated reciprocal allosteric activation—Rabaptin-5 enhances Rabex-5 GEF activity and depends on Rabex-5 for endosomal recruitment—and that the complex is essential for fusion.

    Evidence Reconstitution with recombinant proteins, in vitro GEF, recruitment, and cell-free fusion assays

    PMID:11452015

    Open questions at the time
    • In vivo necessity of Rabaptin-5 for Rabex-5 targeting later challenged
    • Did not quantify feedback kinetics
  6. 2003 High

    Mapped the bipartite GGA and AP-1 adaptor binding of Rabaptin-5, placing the complex at the interface of endosomal sorting and TGN clathrin coats.

    Evidence Co-IP, GST pulldown, FGPLV motif mutagenesis, GGA1 GAT crystal structure with reciprocal mutants, relocalization assays

    PMID:12505986 PMID:14636058

    Open questions at the time
    • Cargo selectivity conferred by these interactions not defined
    • In vivo significance at TGN vs endosomes not separated
  7. 2004 High

    Showed the complex negatively regulates AP-1/clathrin recycling vesicle formation in a Rab4-dependent, Rab5-independent manner, distinguishing its fusion and recycling roles.

    Evidence In vitro vesicle formation assay with biotinylated receptor, immunodepletion, purified protein add-back, BFA controls

    PMID:15331762

    Open questions at the time
    • Molecular switch between fusion-promoting and recycling-regulating modes unknown
    • Physiological cargo not identified
  8. 2007 Medium

    Revised the GEF-targeting model by showing Rabex-5 reaches endosomes and activates Rab5 in vivo via its own EET domain, independent of Rabaptin-5.

    Evidence Rabex-5 deletion mutagenesis, GFP fluorescence microscopy, cellular Rab5-GTP activation assays

    PMID:17699593

    Open questions at the time
    • Reconciliation of in vitro requirement vs in vivo dispensability incomplete
    • Does not exclude amplifying role of Rabaptin-5
  9. 2010 Medium

    Formalized the Rabex-5/Rabaptin-5 positive feedback loop as a delayed, threshold-dependent amplifier of Rab5 activation.

    Evidence Kinetic cell-based measurements with varying Rabex-5 levels integrated with mathematical modeling

    PMID:20169068

    Open questions at the time
    • Model parameters from single system
    • Physiological conditions engaging the indirect pathway not defined
  10. 2012 High

    Identified PKD phosphorylation of Ser407 as a switch directing Rabaptin-5 toward Rab4-dependent short-loop integrin recycling that drives directed cell migration.

    Evidence In vitro kinase assay, phospho-antibodies, S407A/S407D mutagenesis, Rab4/Rab5 co-IP, integrin recycling, migration and invasion assays

    PMID:22975325

    Open questions at the time
    • Structural basis for phospho-dependent Rab4 preference not solved
    • Upstream signals controlling PKD targeting context-specific
  11. 2008 Medium

    Revealed a fusion-independent role: Rabaptin-5 stabilizes cell-surface receptors, tuning immune cell sensitivity.

    Evidence shRNA knockdown in mast cells, flow cytometry of surface FcεRI/β1 integrin, endocytosis and mediator release assays

    PMID:18698003

    Open questions at the time
    • Molecular basis of surface stabilization unresolved
    • Single cell type
  12. 2021 Medium

    Placed Rabaptin-5 under negative control by HD-PTP/PTPN23, coordinating Rab5 deactivation and dephosphorylation with ESCRT-dependent MVB cargo sorting.

    Evidence Direct co-IP with domain mapping, ESCRT-III peptide competition, HD-PTP siRNA, Rab5-GTP and phosphorylation analyses

    PMID:34657963

    Open questions at the time
    • Whether HD-PTP recruits a phosphatase or competes sterically not fully resolved
    • Single lab
  13. 2025 Medium

    Demonstrated an in vivo physiological requirement for RABEP1 recycling activity in neutrophil chemotaxis via Rac/PAK and leading-edge actin.

    Evidence Neutrophil-specific zebrafish knockout, dHL-60 siRNA, domain-deletion rescue, dominant-negative Rab4/Rab5, PAK phospho and F-actin assays

    PMID:40463167 PMID:41701563

    Open questions at the time
    • Link between recycled cargo and Rac activation not molecularly defined
    • Single lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • How RABEP1 isoforms and post-translational state (phosphorylation, cleavage) are integrated to switch between Rab5-fusion, Rab4-recycling, and TGN/ciliary trafficking functions in a given cell context remains unresolved.
  • No structure of full-length dimer bound to both Rab4 and Rab5
  • Isoform-specific (δ, γ) physiological roles uncharacterized
  • Mendelian disease association absent from this corpus

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 3 GO:0060090 molecular adaptor activity 2 GO:0008092 cytoskeletal protein binding 1
Localization
GO:0005794 Golgi apparatus 3 GO:0005768 endosome 2 GO:0005829 cytosol 1
Pathway
R-HSA-5653656 Vesicle-mediated transport 3 R-HSA-9609507 Protein localization 3 R-HSA-162582 Signal Transduction 2
Partners
AP1G1GAP43GGA1ITSN2PTPN23RAB4ARAB5ARABGEF1
Complex memberships
Rabaptin-5/Rabex-5 complex

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 Rabaptin-5 (RABEP1) is a direct effector of GTP-bound Rab5 that is required for early endosome membrane docking and fusion. It is mainly cytosolic but colocalizes with Rab5 on early endosomes; Rab5 recruits it to purified early endosomes in a GTP-dependent manner, and immunodepletion of rabaptin-5 from cytosol strongly inhibits Rab5-dependent early endosome fusion. Co-immunoprecipitation, immunodepletion from cytosol, in vitro endosome fusion assay with purified early endosomes, overexpression with morphological readout (endosome enlargement) Cell High 8521472
1997 Rabaptin-5 forms a tight physical complex with Rabex-5, a novel 60 kDa Rab5 GDP/GTP exchange factor homologous to yeast Vps9p. This complex is essential for endocytic membrane fusion; Rabex-5 displays GDP/GTP exchange activity on Rab5 upon membrane delivery, and the complex stabilizes Rab5 in the GTP-active state. Nanoelectrospray mass spectrometry identification, biochemical co-purification, in vitro nucleotide exchange assay, cell-free endosome fusion assay Cell High 9323142
1997 Rabaptin-5 is cleaved by caspase-family proteases during apoptosis, and this selective cleavage is responsible for the block in endosome fusion observed in apoptotic cells. Cleavage was shown in a cell-free Xenopus egg-extract apoptosis system and in cellular apoptosis models; Bcl-2/Bcl-xL or caspase inhibitors prevented both cleavage and fusion inhibition. Cell-free Xenopus egg-extract apoptosis system, immunoblot detection of cleavage, caspase inhibitors, Bcl-2/Bcl-xL rescue, endosome fusion assay The EMBO journal High 9321397
1998 Rabaptin-5 contains two distinct Rab-binding domains: a 73-residue C-terminal region necessary and sufficient for interaction with GTP-bound Rab5 and Rab5-dependent recruitment to early endosomes, and an N-terminal domain that mediates direct interaction with GTP-bound Rab4. Native cytosolic Rabaptin-5 exists as a homodimer dependent on its coiled-coil sequences. Deletion mutagenesis, GST pulldown assays, yeast two-hybrid, immunofluorescence colocalization, gel filtration (native complex analysis) The EMBO journal High 9524117
1998 Rabaptin-5 interacts with the neuronal growth-associated protein GAP-43 in a Ca2+-dependent manner, and this interaction modulates endocytosis and synaptic vesicle recycling in neurons. Yeast two-hybrid, co-immunoprecipitation, endocytosis assays in neuronal cells, overexpression studies The Journal of neuroscience Medium 9742146
2001 When physically associated in a complex, Rabaptin-5 increases the nucleotide exchange activity of Rabex-5 on Rab5. Rab5-dependent recruitment of Rabaptin-5 to early endosomes is completely dependent on its physical association with Rabex-5, and complex formation is essential for early endosome homotypic fusion. Reconstitution with recombinant proteins, in vitro GEF assay, endosome recruitment assay, cell-free endosome fusion assay Molecular biology of the cell High 11452015
2001 Rabaptin-5 interacts with Rab33b (a Golgi-specific Rab) in its GTP-bound form, suggesting Rabaptin-5 functions not only in the endocytic pathway but also at the Golgi. The interaction was demonstrated by GST-Rab33b pulldown with detection by Western blot and mass spectrometry. GST-Rab33b (GTP-locked) pulldown, Western blot, mass spectrometry FEBS letters Low 11718716
2001 Rabphilin dissociated from Rab3 promotes endocytosis through direct interaction with Rabaptin-5. The Rabphilin V61A mutant (unable to bind Rab3) interacts with Rabaptin-5 and enhances transferrin internalization, whereas Rabphilin L83A fails to bind Rabaptin-5 and does not stimulate endocytosis. Co-immunoprecipitation, transferrin endocytosis assay, point-mutant analysis, overexpression in secretory cells Journal of cell science Medium 11309205
2002 Gamma1-adaptin (a subunit of the AP-1 clathrin adaptor complex at the TGN) directly interacts with Rabaptin-5 through its ear domain binding to the C-terminal coiled-coil region of Rabaptin-5. The two proteins colocalize on perinuclear structures (recycling endosomes) and redistribute to cytoplasm upon brefeldin A treatment. Yeast two-hybrid, GST pulldown, co-immunoprecipitation, immunofluorescence colocalization Journal of biochemistry Medium 11872161
2003 GGAs (Arf-dependent clathrin adaptors) interact with the Rabaptin-5-Rabex-5 complex via a bipartite mechanism: GGA-GAE domains recognize the FGPLV sequence (residues 439-443) in Rabaptin-5 (also recognized by gamma1- and gamma2-adaptin ears), while GGA-GAT domains bind the C-terminal coiled-coils of Rabaptin-5. GFP-Rabaptin-5 overexpression shifts GGA1 and associated cargo to enlarged early endosomes. Co-immunoprecipitation, GST pulldown, site-directed mutagenesis of FGPLV motif, immunofluorescence relocalization assay The EMBO journal High 12505986
2003 The GGA1 GAT domain binds Rabaptin-5 through a hydrophobic surface patch on its C-terminal three-helix bundle. The N284S mutation in this patch reduces Rabaptin-5 binding, and the reciprocal S293N mutation in GGA3 partially confers Rabaptin-5 binding; binding of GAT to Rabaptin-5 is independent of its interaction with ARF. Crystal structure of GGA1 GAT domain, site-directed mutagenesis, in vitro binding assays Biochemistry High 14636058
2004 Rabaptin-5/Rabex-5 complex negatively regulates AP-1/clathrin-coated vesicle formation from endosomes in a Rab4-dependent recycling pathway. Depletion of rabaptin-5/rabex-5 from cytosol stimulated recycling vesicle production, while addition of purified protein strongly inhibited it; Rab4, but not Rab5, was required for this process. In vitro vesicle formation assay using surface-biotinylated receptor, immunodepletion from cytosol, add-back of purified protein, brefeldin A inhibition Molecular biology of the cell High 15331762
2005 The Rabaptin-5δ isoform interacts with GTP-bound Rab5 but not with Rab4, unlike full-length Rabaptin-5 which binds both. This is due to a disrupted Rab4 binding site caused by the alternative splicing deletion, confirmed by yeast two-hybrid, GST pulldown, and immunofluorescence colocalization. Yeast two-hybrid, GST pulldown, immunofluorescence colocalization in BHK-21 cells The FEBS journal Medium 15634330
2006 Rabaptin-5 exists as a dimer in cells, and its δ and γ isoforms also form dimers, providing the first direct evidence for Rabaptin-5 dimerization in a cellular context. Dimerization was established using biochemical cross-linking and co-immunoprecipitation approaches. Co-immunoprecipitation, cross-linking, biochemical fractionation Biochemistry. Biokhimiia Low 17223781
2006 Rabaptin-5γ and Rabaptin-5δ isoforms are cleaved by caspase-3-related proteases in apoptotic cell extracts, and both contain an N-terminal Rab5 binding site that becomes physically separated from the C-terminal Rab5 binding site after apoptotic cleavage, providing a mechanistic model for inactivation of endosome fusion. In vitro cleavage by caspase-3 in cell extracts, immunoblot detection of cleavage products, mapping of Rab5 binding sites on deletion mutants Cell cycle (Georgetown, Tex.) Medium 16861912
2007 Rabex-5 can target to early endosomes and activate Rab5 in vivo via an early endosomal targeting (EET) domain (residues 81-230) that is independent of its Rabaptin-5-binding domain; Rabaptin-5 is therefore not required for Rabex-5 membrane targeting and Rab5 activation in vivo, despite being required in vitro. Deletion mutagenesis of Rabex-5, fluorescence microscopy of GFP-tagged constructs, Rab5-GTP activation assays in cells Molecular biology of the cell Medium 17699593
2008 In mast cells, Rabaptin-5 knockdown reduces surface expression of FcεRI and β1 integrin (by diminishing receptor surface stability) but does not impair FcεRI internalization or endosome fusion. This receptor surface stabilization function of Rabaptin-5 reduces mast cell sensitivity to antigen-induced mediator release and Ag-induced adhesion/migration. shRNA knockdown, flow cytometry for surface receptor levels, transferrin endocytosis assay, mediator release assay Blood Medium 18698003
2010 The Rabex-5/Rabaptin-5 complex forms a positive feedback loop for Rab5 activation on endosomal membranes: Rabaptin-5 binding to Rab5-GTP recruits the Rabex-5/Rabaptin-5 complex to the membrane, where Rabex-5 generates more Rab5-GTP. This indirect pathway has a delayed onset ('delayed response') requiring above-endogenous levels of Rab5 or Rabex-5 to engage. Mathematical modeling, kinetic analysis of Rab5 activation in cells with varying Rabex-5 expression levels, fluorescence assays PloS one Medium 20169068
2012 Protein kinase D (PKD) phosphorylates Rabaptin-5 at Ser407, and this phosphorylation is necessary and sufficient for PDGF-dependent short-loop recycling of αvβ3 integrin. Phosphorylated Rabaptin-5 interacts preferentially with Rab4 (not Rab5) near the front of migrating cells to deliver αvβ3 to the leading edge, driving persistent cell migration and invasion, while also inhibiting α5β1 recycling. In vitro kinase assay (PKD phosphorylation of Rabaptin-5), phospho-specific antibodies, site-directed mutagenesis (S407A/S407D), co-immunoprecipitation with Rab4/Rab5, integrin recycling assays, 2D migration and invasion assays Developmental cell High 22975325
2012 KV10.1 potassium channel physically interacts with Rabaptin-5 and colocalizes on large early endosomes induced by Rab5 hyperactivity. Silencing Rabaptin-5 reduces recycling of KV10.1 to the cell surface and decreases KV10.1 current density in cells natively expressing the channel. Co-immunoprecipitation, immunofluorescence colocalization, siRNA knockdown, whole-cell patch-clamp recording FEBS letters Medium 22841712
2013 In Drosophila, Rabaptin-5 functions as a neoplastic tumor suppressor; loss-of-function mutants cause epithelial disruption and over-proliferation associated with upregulation of JNK and JAK/STAT signaling, without disruption of apico-basal polarity. Its ability to bind Rab5, modulate early endosomal dynamics, and interact with Rabex-5 is conserved in Drosophila. Genetic mosaic analysis in Drosophila (loss-of-function mutations), epistasis with JNK/JAK-STAT pathway reporters, Rab5 binding assays Developmental biology Medium 24104056
2014 Rabep1 couples the polycystin complex (PC1/PC2) to a GGA1/Arl3-based ciliary trafficking module at the TGN, enabling ciliary targeting of these large transmembrane proteins. This was identified by yeast two-hybrid screening and validated with a candidate approach. Yeast two-hybrid screening, co-immunoprecipitation, candidate interaction validation, knockdown with ciliary localization readout Nature communications Medium 25405894
2014 The Rabaptin-5γ isoform, despite its ability to interact with Rab5, is absent from early endosomes and is instead localized to the trans-Golgi network and a Rab4-positive compartment, indicating it functions in membrane transport steps other than Rab5-driven early endosome fusion. Immunofluorescence microscopy, subcellular fractionation, Rab5/Rab4 co-localization analysis in transfected cells Biochemistry. Biokhimiia Low 25385014
2014 HDAC6 overexpression in gastric cancer inhibits rabaptin-5-mediated early endosome fusion, thereby prolonging EGFR activation and sustaining growth stimulation. HDAC6 knockdown caused inhibition of gastric cancer cell growth associated with decreased EGFR signaling. HDAC6 shRNA knockdown, EGFR signaling assays, endosome fusion assays, cell growth assays Cancer letters Low 25111897
2015 ITSN2L (Intersectin-2Long) interacts with Rabaptin-5 (RABEP1) via its CC domain binding to the CC3 region of RABEP1. ITSN2L overexpression promotes RABEP1 degradation and represses RABEP1-enhanced endosome aggregation, functioning as a negative regulator of RABEP1 in endocytosis. Yeast two-hybrid, GST pulldown, co-immunoprecipitation, colocalization microscopy, overexpression with endosome morphology readout International journal of molecular sciences Medium 26633357
2021 HD-PTP (PTPN23) binds directly to Rabaptin-5 between its Rabex-5- and Rab5-binding domains, at the same site that interacts with ESCRT-0/ESCRT-III. HD-PTP depletion leads to Rabaptin-5-dependent hyperactivation of Rab5 and accumulation of hyperphosphorylated Rabaptin-5, blocking cargo exit from Rab5-rich endosomes. This indicates HD-PTP coordinates MVB sorting with endosomal maturation by modulating Rabex-5-Rabaptin-5 activity. Co-immunoprecipitation (direct binding), siRNA depletion of HD-PTP, phosphorylation analysis of Rabaptin-5, Rab5-GTP activation assay, ESCRT-III peptide competition binding assay Journal of cell science Medium 34657963
2025 RABEP1 is essential for neutrophil motility and chemotaxis. In RABEP1-deficient zebrafish and human dHL-60 cells, endosomal recycling is impaired, PAK phosphorylation (Rac activation readout) is reduced, and leading-edge F-actin polymerization is decreased, without affecting Rab5-GTP levels or chemokine-induced cell polarization. Re-expression of full-length RABEP1, but not a truncation lacking the Rab4/Rab5 binding domain, rescues motility. Dominant-negative Rab4 or Rab5 similarly inhibit neutrophil migration. Neutrophil-specific knockout in zebrafish, siRNA knockdown in dHL-60 cells, rescue with domain deletion mutants, dominant-negative Rab4/Rab5 expression, PAK phosphorylation assay, F-actin staining, recycling assays Journal of leukocyte biology Medium 40463167 41701563

Source papers

Stage 0 corpus · 39 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1997 A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 501 9323142
1995 Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 411 8521472
1998 Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5. The EMBO journal 195 9524117
2001 Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex. Molecular biology of the cell 172 11452015
2003 Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex. The EMBO journal 131 12505986
2001 Rabaptin-5 is a novel fusion partner to platelet-derived growth factor beta receptor in chronic myelomonocytic leukemia. Blood 103 11588050
2001 Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER. FEBS letters 102 11718716
2014 Ciliary membrane proteins traffic through the Golgi via a Rabep1/GGA1/Arl3-dependent mechanism. Nature communications 97 25405894
1998 The neuronal growth-associated protein GAP-43 interacts with rabaptin-5 and participates in endocytosis. The Journal of neuroscience : the official journal of the Society for Neuroscience 79 9742146
2004 In vitro formation of recycling vesicles from endosomes requires adaptor protein-1/clathrin and is regulated by rab4 and the connector rabaptin-5. Molecular biology of the cell 72 15331762
1997 Cleavage of rabaptin-5 blocks endosome fusion during apoptosis. The EMBO journal 67 9321397
2012 PKD controls αvβ3 integrin recycling and tumor cell invasive migration through its substrate Rabaptin-5. Developmental cell 50 22975325
2002 Gamma-adaptin interacts directly with Rabaptin-5 through its ear domain. Journal of biochemistry 45 11872161
2007 Rabaptin-5-independent membrane targeting and Rab5 activation by Rabex-5 in the cell. Molecular biology of the cell 42 17699593
2014 HDAC6 sustains growth stimulation by prolonging the activation of EGF receptor through the inhibition of rabaptin-5-mediated early endosome fusion in gastric cancer. Cancer letters 27 25111897
2000 Expression of the endocytosis regulatory proteins Rab5 and Rabaptin-5 in glial cytoplasmic inclusions from brains with multiple system atrophy. Clinical neuropathology 23 10749284
2001 Rabphilin dissociated from Rab3 promotes endocytosis through interaction with Rabaptin-5. Journal of cell science 22 11309205
2010 Delayed onset of positive feedback activation of Rab5 by Rabex-5 and Rabaptin-5 in endocytosis. PloS one 21 20169068
2005 Expression of calpastatin, minopontin, NIPSNAP1, rabaptin-5 and neuronatin in the phenylketonuria (PKU) mouse brain: possible role on cognitive defect seen in PKU. Neurochemistry international 19 15863237
2013 Rabaptin-5 and Rabex-5 are neoplastic tumour suppressor genes that interact to modulate Rab5 dynamics in Drosophila melanogaster. Developmental biology 18 24104056
2003 The interaction of the human GGA1 GAT domain with rabaptin-5 is mediated by residues on its three-helix bundle. Biochemistry 17 14636058
2012 Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion channel trafficking. FEBS letters 16 22841712
2008 Rabaptin-5 regulates receptor expression and functional activation in mast cells. Blood 13 18698003
2005 The Rab5 effector Rabaptin-5 and its isoform Rabaptin-5delta differ in their ability to interact with the small GTPase Rab4. The FEBS journal 13 15634330
2021 His domain protein tyrosine phosphatase and Rabaptin-5 couple endo-lysosomal sorting of EGFR with endosomal maturation. Journal of cell science 12 34657963
2015 The pleckstrin homology domain of phospholipase D1 accelerates EGFR endocytosis by increasing the expression of the Rab5 effector, rabaptin-5. Experimental & molecular medicine 11 26680696
2002 Multiple Rabaptin-5-like transcripts. Gene 10 12119113
2007 Screening of a microvascular endothelial cDNA library identifies rabaptin 5 as a novel autoantigen in Alzheimer's disease. Journal of neuroimmunology 8 17961730
2006 Apoptotic cleavage of rabaptin-5-like proteins and a model for rabaptin-5 inactivation in apoptosis. Cell cycle (Georgetown, Tex.) 7 16861912
2022 The Rabep1-Mediated Endocytosis and Activation of Trypsinogen to Promote Pancreatic Stellate Cell Activation. Biomolecules 5 36008957
2015 ITSN2L Interacts with and Negatively Regulates RABEP1. International journal of molecular sciences 5 26633357
2022 Identification of JPX-RABEP1 Pair as an Immune-Related Biomarker and Therapeutic Target in Pulmonary Arterial Hypertension by Bioinformatics and Experimental Analyses. International journal of molecular sciences 4 36555200
2001 Identification of active regions for neurite outgrowth activity of neurocrescin. Biochemical and biophysical research communications 4 11237723
2005 Analysis of the interaction between GGA1 GAT domain and Rabaptin-5. Methods in enzymology 2 16473621
2006 Dimerization properties of Rabaptin-5 and its isoforms. Biochemistry. Biokhimiia 1 17223781
2026 RABEP1 regulates neutrophil migration via endosomal recycling and actin polymerization. Journal of leukocyte biology 0 41701563
2025 RABEP1 amplifies front signaling in neutrophil migration. bioRxiv : the preprint server for biology 0 40463167
2014 Characterization of Rabaptin-5 γ isoform. Biochemistry. Biokhimiia 0 25385014
2004 Neurocrescin is specifically cleaved after the sequence DESD in a caspase-3-independent manner. Cellular and molecular neurobiology 0 15672675

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