Affinage

RAB11FIP2

Rab11 family-interacting protein 2 · UniProt Q7L804

Length
512 aa
Mass
58.3 kDa
Annotated
2026-06-10
25 papers in source corpus 19 papers cited in narrative 19 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

RAB11FIP2 is a class I Rab11 effector that couples the Rab11-positive endocytic recycling compartment to actin- and microtubule-based vesicle transport, governing the export and recycling of membrane cargo to the cell surface (PMID:11994279, PMID:19542231). Its C-terminal domain forms a parallel homodimer coiled-coil, but coiled-coil formation and Rab11 binding are genetically and structurally separable functions, with the Rab11-binding domain alone necessary and sufficient for early endosomal membrane association (PMID:11994279, PMID:16734419). With Rab11a and the actin motor myosin Vb it assembles a tripartite platform, anchored through FIP2 residues S229/G233, that tethers and stabilizes recycling vesicles; disrupting any component impairs cargo export such as cholesterol-dependent NPC1L1 translocation and increases the speed and track length of Rab11a vesicles (PMID:19542231, PMID:24372966). This platform acts at distinct steps of the recycling pathway, from vesicle formation at the recycling compartment to docking and fusion at the plasma membrane, and supports cargo including AQP2 and apical transcytotic traffic (PMID:22420646, PMID:17156409, PMID:17626244). The N-terminal C2 domain is dispensable for membrane budding and is specifically required for late membrane scission/budding events, including ESCRT-independent respiratory syncytial virus budding (PMID:18621683). A separate regulatory axis is set by MARK2 phosphorylation of Ser-227, which controls epithelial polarity and junction composition and recruits Eps15 through FIP2 NPF motifs to direct lateral membrane organization and single-lumen formation, independently of Rab11a or myosin Vb (PMID:22553350, PMID:28228550). FIP2 also engages the endocytic machinery through NPF-motif and adaptor interactions with Reps1, EHD1/EHD3, and AP-2 (PMID:12364336, PMID:16251358). Beyond canonical recycling, FIP2 acts as a Rab11-independent retention factor that sequesters AMPA receptors away from synaptic surfaces and is mobilized and dephosphorylated during LTP, and controls NLRP3 inflammasome activation by binding NLRP3 via its C2 domain and acting through Rab11b and PI4P-positive compartments [PMID:31757887, PMID:bio_10.1101_2025.05.19.654879].

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 2002 High

    Established RAB11FIP2 as a Rab11-specific effector and localized its membrane-targeting and trafficking functions to defined domains, answering where in the endocytic pathway it acts.

    Evidence Deletion mutagenesis, subcellular fractionation, and dominant-negative overexpression in HeLa cells

    PMID:11994279

    Open questions at the time
    • Did not resolve the role of the C2 domain
    • Cargo specificity not defined
  2. 2002 Medium

    Connected FIP2 to the early endocytic adaptor machinery, showing it forms complexes with Reps1 and AP-2 alpha-adaptin and selectively suppresses EGFR but not transferrin receptor internalization.

    Evidence Co-immunoprecipitation, overexpression, and receptor internalization assays in cell lines

    PMID:12364336

    Open questions at the time
    • NPF-motif dependence of these interactions not dissected
    • Single lab
  3. 2005 High

    Identified EHD1/EHD3 as NPF-motif partners and showed EHD3 is required for delivery of recycling cargo and for proper localization of both FIP2 and Rab11 to the recycling compartment.

    Evidence Reciprocal Co-IP, siRNA knockdown, and transferrin recycling assays

    PMID:16251358

    Open questions at the time
    • Direct structural basis of EH-NPF binding not resolved
    • Functional hierarchy with other adaptors unclear
  4. 2006 High

    Defined the biophysical architecture of the FIP2 C-terminus, demonstrating it is a parallel coiled-coil homodimer and that coiled-coil formation and Rab11 binding are separable activities.

    Evidence Limited proteolysis, cross-linking, sedimentation equilibrium, CD, and ITC with mutagenesis

    PMID:16734419

    Open questions at the time
    • No atomic structure of the complex reported
    • Functional consequence of conformational change in cells untested
  5. 2006 Medium

    Provided solution stoichiometry for the Rab11–FIP2 complex, indicating a 2:2 assembly consistent with the homodimeric coiled-coil.

    Evidence Protein purification, crystallization, and static light scattering

    PMID:16820696

    Open questions at the time
    • No solved high-resolution structure
    • Preliminary diffraction only
  6. 2006 Medium

    Demonstrated a physiological cargo role by showing the C2 domain is required for AVP-stimulated AQP2 plasma membrane redistribution in collecting duct cells, in a Rab11-binding-dependent manner.

    Evidence Dominant-negative C2 deletion with co-localization in AQP2-expressing cells and primary principal cells

    PMID:17156409

    Open questions at the time
    • Direct biochemical activity of the C2 domain not defined
    • Single lab
  7. 2007 Medium

    Distinguished separable trafficking steps using point mutants, showing R413G/SARG mutants impair apical transcytosis distinct from the C2-dependent step without altering known partner interactions.

    Evidence Site-directed mutagenesis and transcytosis assays in polarized MDCK cells

    PMID:17626244

    Open questions at the time
    • Molecular cause of the tubular cisternal phenotype unresolved
    • Single lab
  8. 2008 Medium

    Showed the FIP2 C2 domain is required for the final membrane budding step of RSV, establishing a budding/scission role independent of the ESCRT machinery.

    Evidence Domain-specific dominant-negative overexpression with quantitative viral titer readouts in polarized epithelial cells

    PMID:18621683

    Open questions at the time
    • Direct membrane-deforming activity of C2 not reconstituted
    • Generalizability to cellular budding events untested
  9. 2009 Medium

    Defined the tripartite myosin Vb·Rab11a·FIP2 complex as the functional unit for actin-dependent cargo export, exemplified by NPC1L1 translocation and cholesterol uptake.

    Evidence Three-component dominant-negative epistasis with cholesterol uptake assays and actin disruption

    PMID:19542231

    Open questions at the time
    • Stoichiometry and assembly order of the tripartite complex not defined
    • Single lab
  10. 2011 Low

    Linked FIP2 mutants to microtubule-dependent centripetal endosome movement via dynein co-localization and distinguished C2- versus SARG-dependent endosomal sorting steps.

    Evidence Dominant-negative overexpression and co-localization in polarized MDCK cells

    PMID:21686255

    Open questions at the time
    • Single method (co-localization) with no direct binding or rescue
    • Dynein interaction not biochemically validated
  11. 2012 Medium

    Resolved the spatiotemporal logic of the myosin Vb/Rab11a/FIP2 platform, showing it acts sequentially at vesicle formation in the recycling compartment and at docking/fusion at the plasma membrane.

    Evidence Live-FRET, FRAP, fast confocal, and TIRF microscopy of langerin recycling in live cells

    PMID:22420646

    Open questions at the time
    • Molecular triggers of the temporal switch unknown
    • Single lab
  12. 2012 High

    Uncovered a Rab11-independent regulatory function in which MARK2 phosphorylation of Ser-227 governs epithelial polarity and junction composition.

    Evidence Phospho-mimetic/non-phosphorylatable mutants in 3D MDCK cyst culture with junction marker analysis

    PMID:22553350

    Open questions at the time
    • Downstream effectors of pS227 not all identified
    • Direct MARK2-FIP2 kinetics not characterized
  13. 2014 High

    Mapped the myosin Vb interaction to residues S229/G233 and showed this tether stabilizes Rab11a vesicle movement, mechanistically grounding the tripartite platform.

    Evidence Random mutagenesis, yeast two-hybrid, Co-IP, and live-cell vesicle tracking in HeLa and MDCK cells

    PMID:24372966

    Open questions at the time
    • Structural basis of the MYO5B-FIP2 interface not solved
    • Regulation of this interaction by phosphorylation untested
  14. 2017 High

    Defined the effector of pS227-FIP2 polarity signaling as Eps15, recruited through FIP2 NPF motifs to direct lateral membrane organization and single-lumen formation.

    Evidence Co-IP, NPF-domain mutagenesis, siRNA knockdown, and 3D cyst culture in MDCK cells

    PMID:28228550

    Open questions at the time
    • How pS227 controls NPF-Eps15 binding mechanistically is unclear
    • Cargo trafficked by this axis not identified
  15. 2017 Medium

    Showed FIP2 is hijacked by Chlamydia pneumoniae to recruit myosin Vb and reposition the inclusion, demonstrating a pathogen-exploited trafficking role.

    Evidence siRNA knockdown, deletion variants, and infection assays with immunofluorescence

    PMID:28787457

    Open questions at the time
    • Bacterial factor engaging FIP2 not identified
    • Single lab
  16. 2018 Low

    Reported a non-trafficking role in which FIP2 binds PGK1 and promotes its ubiquitination to dampen AKT/mTOR signaling in lung cancer cells.

    Evidence Co-IP, ubiquitination assay, and overexpression in NSCLC cells

    PMID:30471866

    Open questions at the time
    • No E3 ligase identified and no in vitro reconstitution
    • Single lab, not independently confirmed
  17. 2019 Medium

    Established a Rab11-independent function as an AMPA receptor retention factor whose mobilization and dephosphorylation are required for synaptic potentiation.

    Evidence shRNA knockdown, Co-IP, and live imaging in rat hippocampal slices

    PMID:31757887

    Open questions at the time
    • Phosphatase mediating LTP-induced dephosphorylation not identified
    • Direct FIP2-GluA1 binding interface unmapped
  18. 2019 Low

    Linked FIP2 to nasopharyngeal carcinoma migration/invasion through Rac and Cdc42 expression.

    Evidence siRNA knockdown, migration/invasion assays, and western blot in cancer cells

    PMID:31452257

    Open questions at the time
    • No direct mechanistic link between FIP2 and Rho GTPase regulation
    • Single method, single lab
  19. 2025 Medium

    Implicated FIP2 in innate immunity by showing it controls NLRP3 inflammasome activation through Rab11b, IKKβ/TAK1 signaling, NLRP3 translocation, and PI4P-positive endosomes, binding NLRP3 via its C2 domain.

    Evidence Knockdown, Co-IP, domain mutagenesis, and inflammasome activation assays in human macrophages (preprint)

    PMID:bio_10.1101_2025.05.19.654879

    Open questions at the time
    • Preprint not yet peer-reviewed
    • Mechanism of C2-mediated PI4P/endosome control not defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How FIP2's distinct functional modes — Rab11/myosin Vb tethering, C2-dependent budding, pS227/Eps15 polarity signaling, and Rab11-independent cargo retention — are coordinated and switched within a single cell remains unresolved.
  • No high-resolution structure of any full-length complex
  • Regulation integrating phosphorylation and partner selection unknown
  • In vivo physiological phenotypes largely uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0008092 cytoskeletal protein binding 2 GO:0008289 lipid binding 2
Localization
GO:0005768 endosome 3 GO:0031410 cytoplasmic vesicle 3 GO:0005829 cytosol 2 GO:0005886 plasma membrane 2
Pathway
R-HSA-5653656 Vesicle-mediated transport 4 R-HSA-9609507 Protein localization 2 R-HSA-168256 Immune System 1
Partners
EHD3EPS15MARK2MYO5BNLRP3RAB11ARAB11BREPS1
Complex memberships
Rab11a·myosin Vb·RAB11FIP2 tripartite recycling complex

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 Rab11-FIP2 specifically interacts with Rab11 but not Rab4, Rab3, Rab5, Rab6, or Rab7. The COOH-terminal region containing the Rab11 binding domain (RBD) is necessary and sufficient for early endosomal membrane association, while the N-terminal C2 domain alone is insufficient for membrane binding. Expression of an RBD-containing deletion mutant causes tubulation of transferrin receptor-positive early endosomes, suggesting Rab11-FIP2 functions downstream of Rab11 in endosomal trafficking. Deletion mutagenesis, subcellular fractionation, immunofluorescence, dominant-negative overexpression in HeLa cells The Journal of biological chemistry High 11994279
2002 Rab11-FIP2 contains an NPF motif that mediates binding to Reps1 (an EH domain protein involved in endocytosis) and also associates with the alpha-adaptin subunit of AP-2. Overexpression of Rab11-FIP2 suppresses EGF receptor internalization but not transferrin receptor internalization, through binding sites that promote complex formation with Rab11, Reps1, and alpha-adaptin. Co-immunoprecipitation, overexpression, receptor internalization assay in cell lines The Journal of biological chemistry Medium 12364336
2005 EHD1 and EHD3 bind to Rab11-FIP2 via EH domain–NPF motif interactions. These associations are affected by the nucleotide-binding state of EHD proteins. Loss of EHD3 prevents delivery of internalized transferrin and early endosomal proteins to the endocytic recycling compartment (ERC), and alters the subcellular localization of Rab11-FIP2 and endogenous Rab11, retaining both in the cell periphery rather than the ERC. Co-immunoprecipitation, siRNA knockdown, immunofluorescence, transferrin recycling assay Molecular biology of the cell High 16251358
2006 The C-terminal domain of Rab11-FIP2 forms a parallel homodimer coiled-coil in solution. Coiled-coil formation and Rab11 binding are separable functions: a construct truncated at the N-terminus of the C-terminal domain retains Rab11 binding affinity but loses structure, while a minimal coiled-coil construct (truncated at C-terminus) is well-structured but cannot bind Rab11. Conformational changes occur in Rab11-FIP2 upon Rab11 complex formation. Limited proteolysis, cross-linking, sedimentation equilibrium, circular dichroism, isothermal titration calorimetry, mutagenesis Biochemistry High 16734419
2006 Rab11-FIP2 co-localizes with AQP2 in renal collecting duct cells. A dominant-negative Rab11-FIP2 lacking the C2 domain (Rab11-FIP2-ΔC2) disrupts recycling and causes condensation of AQP2 in a Rab11-positive compartment, abolishing AVP-stimulated AQP2 plasma membrane redistribution (the AQP2 shuttle). This effect requires binding of Rab11-FIP2-ΔC2 to Rab11. Dominant-negative overexpression, immunofluorescence, co-localization in AQP2-expressing cell lines and primary principal cells Traffic (Copenhagen, Denmark) Medium 17156409
2006 A complex of Rab11 and the RBD of Rab11-FIP2 was crystallized; static light-scattering analyses indicate the complex contains two copies of Rab11 and two copies of Rab11-FIP2 in solution, consistent with a 2:2 stoichiometry. Protein purification, crystallization, static light scattering Acta crystallographica. Section F, Structural biology and crystallization communications Medium 16820696
2007 Point mutant Rab11-FIP2(R413G) or Rab11-FIP2(S229A/R413G) causes formation of a tubular cisternal structure containing Rab11a and decreases the rate of polymeric IgA transcytosis in polarized MDCK cells, without altering interactions with known binding partners. Different Rab11-FIP2 mutants (ΔC2 vs. SARG) distinguish distinct steps of the apical recycling pathway. Site-directed mutagenesis, overexpression in polarized MDCK cells, transcytosis assay, immunofluorescence American journal of physiology. Cell physiology Medium 17626244
2008 A dominant-negative form of Rab11-FIP2 lacking its N-terminal C2 domain reduced supernatant-associated RSV titer 1,000-fold while increasing cell-associated virus titer, indicating FIP2 C2 domain is required for the final RSV budding step. Truncation of the Rab-binding domain from FIP2 caused accumulation of FIP2 in mature filamentous virions. RSV budding was shown to be independent of the ESCRT machinery. Dominant-negative overexpression, viral titer measurement, immunofluorescence in polarized epithelial cells Proceedings of the National Academy of Sciences of the United States of America Medium 18621683
2009 Rab11-FIP2 forms a tripartite complex with myosin Vb and Rab11a that is required for cholesterol-regulated translocation of NPC1L1 from the endocytic recycling compartment to the plasma membrane. Dominant-negative mutants of any component of the myosin Vb·Rab11a·Rab11-FIP2 complex inhibit NPC1L1 export and decrease cellular cholesterol uptake. Dominant-negative overexpression, cholesterol uptake assay, immunofluorescence, pharmacological actin disruption The Journal of biological chemistry Medium 19542231
2011 Rab11-FIP2 mutants (ΔC2 and SARG) both alter localization and co-localize with dynein heavy chain, suggesting involvement in microtubule-dependent centripetal movement of endosomes. ΔC2 but not SARG causes clustering of early endosomal markers Rab5b, Epsin 4, and IQGAP1, while SARG but not ΔC2 causes accumulation of clathrin heavy chain and AP-1 at membranes. Dominant-negative overexpression, immunofluorescence, co-localization in polarized MDCK cells Cellular logistics Low 21686255
2012 Rab11-FIP2 is phosphorylated on Ser-227 by MARK2, and this phosphorylation regulates epithelial cell polarity. Non-phosphorylatable S227A mutant causes loss of lumen formation in MDCK cysts; pseudophosphorylated S227E mutant induces multiple lumens and alters composition of adherens junctions (loss of E-cadherin, retention of p120-catenin and K-cadherin) and tight junctions (loss of occludin, altered claudin composition). These polarity effects do not require myosin Vb or Rab11a. Site-directed mutagenesis (S227A, S227E), 3D Matrigel cyst culture, immunofluorescence, western blot in MDCK cells Molecular biology of the cell High 22553350
2012 The Myosin Vb/Rab11A/Rab11-FIP2 platform regulates langerin recycling at two distinct sites: first at the sorting site in the endosomal recycling compartment (ERC) where transport vesicles are formed, and subsequently at the late stage of docking/tethering and fusion of recycling vesicles to the plasma membrane, in a strict temporal order. Live-FRET, fast FRAP video, fast confocal microscopy, TIRF microscopy in live cells Traffic (Copenhagen, Denmark) Medium 22420646
2014 Specific residues S229 and G233 in Rab11-FIP2 are required for interaction with MYO5B. Disruption of the MYO5B/Rab11-FIP2 association (by mutation S229P/G233E or Rab11-FIP2 knockdown) increases Rab11a-containing vesicle speed and track length, consistent with impaired MYO5B tethering at the cytoskeleton, supporting the role of this interaction in stabilizing the Rab11a functional complex. Random mutagenesis, yeast two-hybrid, co-immunoprecipitation, live-cell vesicle tracking (HeLa and MDCK cells), siRNA knockdown Traffic (Copenhagen, Denmark) High 24372966
2017 MARK2-phosphorylated Rab11-FIP2 (pS227-FIP2) interacts with Eps15 via the NPF domains of FIP2. During recovery of cell polarity, Eps15 localizes to the lateral membrane before pS227-FIP2 arrival, and later they co-localize. Pseudophosphorylated FIP2(S227E) traps Eps15 and prevents its lateral membrane localization; mutation of any of the three NPF domains in FIP2(S227E) rescues Eps15 localization and restores single-lumen cyst formation. Knockdown of Eps15 alters pS227-FIP2 localization and induces multiple lumens. Co-immunoprecipitation, NPF domain mutagenesis, siRNA knockdown, immunofluorescence, 3D cyst culture in MDCK cells Molecular biology of the cell High 28228550
2017 Rab11-FIP2 is recruited to the Chlamydia pneumoniae nascent inclusion upon internalization and retained throughout infection. siRNA knockdown of Rab11-FIP2 impairs C. pneumoniae internalization and infection. Rab11-FIP2 regulates intracellular positioning of the inclusion, and its binding to Rab11 recruits myosin Vb to the early inclusion to regulate relocation from the cell periphery to the perinuclear region. siRNA knockdown, immunofluorescence, expression of deletion variants, infection assay PLoS pathogens Medium 28787457
2018 Rab11-FIP2 interacts with glycolytic kinase PGK1 and promotes its ubiquitination, leading to inactivation of the AKT/mTOR signaling pathway in non-small cell lung cancer cells. Co-immunoprecipitation, ubiquitination assay, overexpression, western blot Biochemical and biophysical research communications Low 30471866
2019 Under basal conditions, RAB11FIP2 (FIP2) associates with AMPA receptors (AMPARs/GluA1) at immobile compartments separately from recycling endosomes, preventing GluA1 from reaching dendritic spine surfaces. Upon LTP induction, FIP2 is rapidly mobilized, dissociates from AMPARs, and undergoes dephosphorylation. This dissociation and FIP2 dephosphorylation are required for LTP, but FIP2-Rab11 interaction is not required for this process. shRNA knockdown, co-immunoprecipitation, live imaging, immunofluorescence in rat hippocampal slices Journal of cell science Medium 31757887
2019 Knockdown of Rab11-FIP2 inhibits migration and invasion of nasopharyngeal carcinoma cells by decreasing expression of Rac and Cdc42 (Rho GTPases), without affecting EMT markers or Akt signaling. siRNA knockdown, migration/invasion assay, western blot for Rho GTPases Journal of cellular biochemistry Low 31452257
2025 Rab11-FIP2 and Rab11b (but not Rab11a) control caspase-1-mediated cleavage of pro-IL-1β and GSDMD and pyroptotic cell death in human macrophages. Rab11-FIP2 controls LPS-stimulated IKKβ activation by TAK1 and IKKβ-mediated NLRP3 translocation to the trans-Golgi network. NLRP3 binds Rab11-FIP2 via its KMKK motif, while Rab11-FIP2 interacts with NLRP3 via its N-terminal C2 domain. Formation of PI4P-positive endosomes and ASC-specks are controlled by Rab11-FIP2. siRNA/shRNA knockdown, co-immunoprecipitation, domain deletion mutagenesis, inflammasome activation assays (IL-1β ELISA, caspase-1 cleavage, pyroptosis), immunofluorescence in human macrophages bioRxivpreprint Medium bio_10.1101_2025.05.19.654879

Source papers

Stage 0 corpus · 25 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early endosomal transport. Molecular biology of the cell 160 16251358
2008 Respiratory syncytial virus uses a Vps4-independent budding mechanism controlled by Rab11-FIP2. Proceedings of the National Academy of Sciences of the United States of America 127 18621683
2006 A Role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle. Traffic (Copenhagen, Denmark) 110 17156409
2002 Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain. The Journal of biological chemistry 99 11994279
2002 Rab11-FIP2, an adaptor protein connecting cellular components involved in internalization and recycling of epidermal growth factor receptors. The Journal of biological chemistry 85 12364336
2017 Exosomal miR-142-3p is increased during cardiac allograft rejection and augments vascular permeability through down-regulation of endothelial RAB11FIP2 expression. Cardiovascular research 82 28073833
2014 Rab11-FIP2 interaction with MYO5B regulates movement of Rab11a-containing recycling vesicles. Traffic (Copenhagen, Denmark) 57 24372966
2009 Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface. The Journal of biological chemistry 57 19542231
2016 Rab11-FIP2 promotes colorectal cancer migration and invasion by regulating PI3K/AKT/MMP7 signaling pathway. Biochemical and biophysical research communications 43 26792722
2012 A Rab11A/myosin Vb/Rab11-FIP2 complex frames two late recycling steps of langerin from the ERC to the plasma membrane. Traffic (Copenhagen, Denmark) 40 22420646
2012 Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells. Molecular biology of the cell 29 22553350
2007 Rab11-FIP2 regulates differentiable steps in transcytosis. American journal of physiology. Cell physiology 29 17626244
2015 Rab11-FIP2 promotes the metastasis of gastric cancer cells. International journal of cancer 27 26502090
2017 Acquisition of Rab11 and Rab11-Fip2-A novel strategy for Chlamydia pneumoniae early survival. PLoS pathogens 22 28787457
2011 Rab11-FIP2 influences multiple components of the endosomal system in polarized MDCK cells. Cellular logistics 22 21686255
2018 Inhibition of the miR-192/215-Rab11-FIP2 axis suppresses human gastric cancer progression. Cell death & disease 21 30006518
2006 Molecular dissection of Rab11 binding from coiled-coil formation in the Rab11-FIP2 C-terminal domain. Biochemistry 17 16734419
2018 Rab11-FIP2 suppressed tumor growth via regulation of PGK1 ubiquitination in non-small cell lung cancer. Biochemical and biophysical research communications 16 30471866
2021 The LncRNA CASC11 Promotes Colorectal Cancer Cell Proliferation and Migration by Adsorbing miR-646 and miR-381-3p to Upregulate Their Target RAB11FIP2. Frontiers in oncology 15 33937069
2018 Overexpression of Rab11-FIP2 in colorectal cancer cells promotes tumor migration and angiogenesis through increasing secretion of PAI-1. Cancer cell international 13 29540997
2019 A retention-release mechanism based on RAB11FIP2 for AMPA receptor synaptic delivery during long-term potentiation. Journal of cell science 8 31757887
2006 Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2. Acta crystallographica. Section F, Structural biology and crystallization communications 8 16820696
2005 Purification and functional properties of Rab11-FIP2. Methods in enzymology 8 16473614
2017 Interaction of phosphorylated Rab11-FIP2 with Eps15 regulates apical junction composition. Molecular biology of the cell 4 28228550
2019 Knockdown Rab11-FIP2 inhibits migration and invasion of nasopharyngeal carcinoma via suppressing Rho GTPase signaling. Journal of cellular biochemistry 3 31452257

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