| 2001 |
RAB11-FIP1 (Rab11-FIP1) was identified as a Rab11a-binding protein that associates with wild-type and dominant-active Rab11a (S20V), as well as Rab11b and Rab25, through a conserved carboxyl-terminal amphipathic alpha-helix. RAB11-FIP1 colocalizes with Rab11a in plasma membrane recycling systems in non-polarized HeLa cells and polarized MDCK cells, and co-enriches with Rab11a and H+K+-ATPase on parietal cell tubulovesicles, translocating with them upon histamine stimulation. |
Co-immunoprecipitation, yeast two-hybrid, colocalization by fluorescence microscopy, subcellular fractionation of parietal cells |
The Journal of biological chemistry |
High |
11495908
|
| 2001 |
Binding of RAB11-FIP1 to Rab11a requires the conserved carboxyl-terminal amphipathic alpha-helix of RAB11-FIP1; this domain is necessary for Rab11 interaction. |
Domain deletion/mutation analysis combined with co-immunoprecipitation |
The Journal of biological chemistry |
High |
11495908
|
| 2003 |
During mitosis in MDCK cells, RAB11-FIP1 dissociates from recycling system markers during late prophase and relocates to the pericentriolar material, then returns to recycling system vesicles during telophase, indicating a cell-cycle-regulated change in subcellular localization distinct from other Rab11 effectors. |
Live-cell and fixed fluorescence microscopy of GFP-tagged RAB11-FIP1 through cell cycle stages, western blot analysis of membrane association |
Traffic (Copenhagen, Denmark) |
Medium |
12956871
|
| 2006 |
The RAB11FIP1 gene encodes eight alternatively spliced transcripts (FIP1A-H); isoforms A-D contain the C-terminal Rab11-binding domain and target to Rab11a-containing recycling membranes when overexpressed in HeLa cells, while isoforms E, F, and H lack the Rab11-binding domain and do not localize to recycling system membranes. Endogenous FIP1C/RCP occupies a partially distinct subcompartment within the recycling system compared to FIP1A and FIP1B. |
Cloning of alternatively spliced transcripts, GFP-fusion overexpression with colocalization microscopy, isoform-specific antibody staining |
Biochimica et biophysica acta |
Medium |
16920206
|
| 2009 |
Overexpression of RCP/RAB11FIP1 in MCF10A normal mammary epithelial cells induces loss of contact inhibition, growth-factor independence, and anchorage-independent growth. Knockdown of RCP in breast cancer cell lines inhibits colony formation, invasion, and migration in vitro and reduces tumor formation and metastasis in mouse xenograft models. Overexpression of RCP enhances ERK phosphorylation and increases Ras activation in vitro. |
Overexpression and shRNA knockdown in cell lines, mouse xenograft tumor models, ERK phosphorylation assay, Ras activation assay |
The Journal of clinical investigation |
High |
19620787
|
| 2013 |
RAB11-FIP1 isoforms (FIP1A, FIP1B, FIP1C) occupy spatially and temporally distinct subdomains within the Rab11a-dependent recycling system; FIP1B reaches maximal transferrin colocalization early (5 min), while FIP1A and FIP1C peak later (≥10 min). FIP1A directly associates with FIP1B and FIP1C, and also associates with FIP3-containing membranes. Rab11-FIP1 proteins form selective pairwise associations on dynamic tubular recycling compartments. |
Live-cell deconvolution fluorescence microscopy of GFP-tagged FIPs, transferrin pulse-chase assay, dual-expression live-cell imaging |
Molecular biology of the cell |
Medium |
23283983
|
| 2013 |
RAB11-FIP1 (FIP1) overexpression decreases adiponectin secretion in HEK293 cells, and shRNA-mediated depletion of FIP1 enhances adiponectin release from 3T3-L1 adipocytes. Endogenous FIP1 co-distributes intracellularly with endogenous adiponectin. FIP1 depletion does not alter transferrin receptor recycling or insulin-mediated Glut4 trafficking. |
Overexpression and shRNA knockdown, adiponectin secretion ELISA, immunofluorescence colocalization, transferrin recycling assay |
PloS one |
Medium |
24040321
|
| 2014 |
RAB11-FIP1 proteins (FIP1A, FIP1B, FIP1C) consistently colocalize with the phosphatidylserine (PS) probe LactC2 along peripheral and pericentriolar compartments. Removal of C2 domains from Rab11-FIPs causes accumulation of LactC2 probe in the pericentriolar region, suggesting that inhibition of recycling affects PS distribution. |
Live-cell fluorescence microscopy and structured illumination microscopy with LactC2-PS biosensor co-expressed with GFP-Rab11-FIPs |
Cellular logistics |
Medium |
25210648
|
| 2016 |
A point mutation at Threonine-197 to Alanine in Rab11-FIP1A acts as a dominant-negative that collapses the normally distributed recycling endosomes into a central membranous cisternum, sequesters endogenous Rab11a, Rab11-FIP1C, and transferrin receptor (CD71), and causes a strong block in transferrin recycling. Rab5 and EEA1 (but not Rab4) accumulate in FIP1A-positive membranes, suggesting a direct pathway from early endosomes into the Rab11a recycling system. |
Site-directed mutagenesis, GFP-fusion overexpression, fluorescence microscopy, transferrin recycling assay, nocodazole treatment |
Experimental cell research |
Medium |
26790954
|
| 2017 |
MARK2 kinase phosphorylates Rab11-FIP1B/C at serine 234 (in a consensus site analogous to the previously identified S227 in Rab11-FIP2). In MDCK cells during calcium-switch-induced repolarization, pS234-FIP1 phosphorylation persists through and after polarity reestablishment. Overexpression of non-phosphorylatable FIP1C(S234A) induces a lateral lumen phenotype with misorientation of apical markers (ezrin, syntaxin 3, podocalyxin), F-actin, ZO1, centrosome, and Golgi apparatus, demonstrating that FIP1 phosphorylation by MARK2 regulates epithelial polarity. |
Phospho-specific antibody generation, kinase assay, calcium-switch repolarization model, overexpression of phospho-mutants with immunofluorescence microscopy |
Cellular logistics |
Medium |
28396819
|
| 2019 |
The ubiquitin ligase RFFL directly ubiquitylates Rab11-FIP1 in vitro, and RFFL knockout specifically reduces ubiquitylation of Rab11-FIP1 (while having minimal effect on ubiquitylation of EHD1, MICALL1, and Rab11-FIP2). RFFL interacts with class I Rab11-FIPs as identified by BioID proximity labeling. A dominant-negative RFFL mutant prolongs interaction with Rab11 effectors including FIP1, induces clustering of endocytic recycling compartments, and delays cargo recycling. |
BioID proximity proteomics, in vitro ubiquitylation assay, RFFL knockout cells, dominant-negative RFFL overexpression, transferrin recycling assay |
Journal of cell science |
High |
30659120
|
| 2021 |
Genetic knockdown of Rab11-FIP1 in esophageal squamous cell carcinoma (ESCC) 3D organoid models increases organoid size and tumor cell invasion. Loss of Rab11-FIP1 in human ESCC cell lines decreases E-cadherin expression and increases mesenchymal markers (EMT). Rab11-FIP1 directly inhibits Zeb1, a key EMT transcription factor, thereby regulating EMT. |
shRNA knockdown, 3D organoid models, invasion assay, western blot for EMT markers, mouse model of ESCC |
EMBO reports |
Medium |
33403789
|
| 2021 |
Rab11-FIP1 and Rab11-FIP5 knockdown additively impairs pIgR/pIgA transcytosis. TRIM21 mediates K11-linked polyubiquitination of Rab11-FIP1 (and K6-linked polyubiquitination of Rab11-FIP5) to promote their activation and facilitate pIgA transcytosis. In incompletely polarized cells, Rab11a-positive endosomes containing pIgR/pIgA, Rab11-FIP1, and Rab11-FIP5 are transported to the apical membrane via the Golgi apparatus. |
siRNA knockdown, co-immunoprecipitation, ubiquitin linkage-specific antibody analysis, transcytosis assay in polarized and incompletely polarized epithelial cells |
International journal of molecular sciences |
Medium |
34638806
|
| 2022 |
Global Rab11FIP1 knockout (KO) mice develop spontaneous colonic inflammation with infiltration of macrophages and neutrophils, reduced TFF3-positive goblet cells, and abnormal accumulation of subapical vesicles in colonocytes. Rab11FIP1 loss causes mistrafficking of transmembrane mucin MUC13, which aberrantly internalizes with Rab14 instead of being properly recycled, resulting in impaired colonic mucosal integrity. |
Global KO mouse generation (exon 2 deletion), immunostaining, RNA-sequencing, DSS colitis model, confocal microscopy |
American journal of physiology. Gastrointestinal and liver physiology |
High |
35819177
|
| 2022 |
CircRTN4 interacts with RAB11FIP1 protein to block its ubiquitination site, thereby stabilizing RAB11FIP1 and preventing its proteasomal degradation. CircRTN4 knockdown promotes RAB11FIP1 degradation by increasing its ubiquitination and decreases EMT marker expression (Slug, Snai1, Twist, Zeb1, N-cadherin) in pancreatic cancer cells. |
circRNA pulldown with mass spectrometry, protein stability assay, ubiquitination assay, 3D structure modeling |
Molecular cancer |
Medium |
34983537
|
| 2023 |
HIF-1-induced upregulation of RCP/RAB11FIP1 under hypoxia promotes Rab11a-dependent recycling of internalized MSC-derived small extracellular vesicles (MSC-sEVs), reducing their intracellular cargo delivery efficiency. RAB11FIP1 enhances the interaction between Rab11a and MSC-sEVs under hypoxic conditions, and siRNA-mediated knockdown of RCP in engineered MSC-sEVs inhibits this recycling, improving cargo delivery. |
siRNA knockdown, co-immunoprecipitation (Rab11a-sEV interaction), rat intervertebral disk degeneration model, fluorescence microscopy of sEV trafficking |
ACS nano |
Medium |
36730125
|
| 2023 |
The transcription factor Stat1 binds to the promoter of Rab11fip1 to initiate Schwann cell differentiation. Stat1 knockdown reduces Rab11fip1 expression and blocks Schwann cell differentiation, thereby inhibiting myelination. |
ChIP-seq, ChIP-qPCR, luciferase reporter assay, siRNA knockdown in Schwann cells, in vivo sciatic nerve model |
Molecular medicine (Cambridge, Mass.) |
Medium |
37365519
|
| 2026 |
RAB11FIP5 competitively sequesters RAB11A to antagonize RAB11FIP1-mediated transferrin and transferrin receptor recycling in HNSCC cells, thereby restricting iron uptake and suppressing ferroptosis. Loss of RAB11FIP5 thus permits RAB11FIP1-mediated recycling, increasing iron uptake and ferroptosis sensitivity. |
RAB11FIP5 knockout cell lines, transferrin recycling assay, iron uptake measurement, ferroptosis assays, subcutaneous xenograft models |
Cell reports |
Medium |
42207639
|