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RAB11 family interacting protein 3
Rab11-FIP3, Rab11-Family Interacting Protein 3, KIAA0665
Proteins of the large Rab GTPase family (see RAB1A; MIM 179508) have regulatory roles in the formation, targeting, and fusion of intracellular transport vesicles. RAB11FIP3 is one of many proteins that interact with and regulate Rab GTPases (Hales et al., 2001 [PubMed 11495908]).[supplied by OMIM, Mar 2008] (from
NCBI)
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Papers on
Rab11-FIP3
Rab11-FIP3 is a cell cycle-regulated phosphoprotein.
Glasgow, United Kingdom. In Bmc Cell Biol, 2011
BACKGROUND: Rab11 and its effector molecule, Rab11-FIP3 (FIP3), associate with recycling endosomes and traffic into the furrow and midbody of cells during cytokinesis.
Distinct roles of Rab11 and Arf6 in the regulation of Rab11-FIP3/arfophilin-1 localization in mitotic cells.
Kyoto, Japan. In Genes Cells, 2011
Rab11 family interacting protein 3/arfophilin-1 is a dual effector of Rab11 and Arf6 and exhibits Rab11-dependent localization to recycling endosomes in interphase.
IKKε regulates cell elongation through recycling endosome shuttling.
Kōbe, Japan. In Dev Cell, 2011
Mammalian IKK-related kinases also regulate the recycling endosomes' distribution by phosphorylating the Nuf homolog Rab11-FIP3.
A novel cytoplasmic adaptor for retinoic acid receptor (RAR) and thyroid receptor functions as a Derepressor of RAR in the absence of retinoic acid.
GeneRIF
Seoul, South Korea. In J Biol Chem, 2010
CART1 might be a cytoplasmic, testis-specific derepressor of RAR
The Rab11 pathway is required for influenza A virus budding and filament formation.
Cambridge, United Kingdom. In J Virol, 2010
We find that cellular Rab11 (a small GTP-binding protein involved in endocytic recycling) and Rab11-family interacting protein 3 ([FIP3] which plays a role in membrane trafficking and regulation of actin dynamics) are both required to support the formation of filamentous virions, while Rab11 is additionally involved in the final budding step of spherical particles.
Rab11-FIP3 binds dynein light intermediate chain 2 and its overexpression fragments the Golgi complex.
GeneRIF
Cork, Ireland. In Biochem Biophys Res Commun, 2010
FIP3 was identified as the first membrane-associated interacting-partner for DLIC-2.
Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport to the endosomal-recycling compartment.
Cork, Ireland. In J Cell Sci, 2010
Here, we show that the Rab11 GTPase effector protein Rab11-FIP3 (henceforth, FIP3) directly interacts with the dynein light intermediate chain 1 (DLIC-1, gene symbol DYNC1LI1) subunit of the cytoplasmic dynein 1 motor protein complex.
Rab11-FIP3 is a Rab11-binding protein that regulates breast cancer cell motility by modulating the actin cytoskeleton.
GeneRIF
Aurora, United States. In Eur J Cell Biol, 2009
Rab11-FIP3 is a Rab11-binding protein that regulates breast cancer cell motility by modulating the actin cytoskeleton.(325-41)
Molecular characterization of Rab11-FIP3 binding to ARF GTPases.
GeneRIF
Aurora, United States. In Eur J Cell Biol, 2007
FIP3 is a scaffolding protein that, in addition to regulating endosome targeting to the cleavage furrow, also is required for Arf6 recruitment to the midbody during late telophase.
Rab11-FIP3 is critical for the structural integrity of the endosomal recycling compartment.
GeneRIF
Cork, Ireland. In Traffic, 2007
Necessary for the structural integrity of the pericentrosomal endosomal recycling compartment.
Novel putative targets of N-ethylmaleimide sensitive fusion protein (NSF) and alpha/beta soluble NSF attachment proteins (SNAPs) include the Pak-binding nucleotide exchange factor betaPIX.
Bristol, United Kingdom. In J Cell Biochem, 2006
A yeast two-hybrid screen using NSF as bait identified Rab11-FIP3 and the Pak-binding nucleotide exchange factor betaPIX as putative binding partners.
Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis.
Glasgow, United Kingdom. In Embo J, 2005
The dual Rab11/Arf binding proteins, family of Rab11-interacting proteins FIP3 and FIP4 function in the delivery of recycling endosomes to the cleavage furrow and are, together with Rab11, essential for completion of abscission, the terminal step of cytokinesis.
The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis.
GeneRIF
Denver, United States. In Mol Biol Cell, 2005
FIP-3 and RAB11 protein complex regulates recycling endosomes targeting to the cleavage furrow during late cytokinesis.
Purification and functional properties of Rab11-FIP3.
In Methods Enzymol, 2004
Rab11-FIP3, a member of this Rab11-binding protein family, in addition to interacting with Rab11, is also capable of interaction with members of the ADP-Ribosylation Factor (ARF) GTPase family.
The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane.
Cork, Ireland. In J Cell Sci, 2004
Rab11-FIP3 and Rab11-FIP4 possess an ezrin-radixin-moesin (ERM) domain in their C-terminal half and EF hands in their N-terminal region.
Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis.
GeneRIF
Cork, Ireland. In Biochem Biophys Res Commun, 2004
Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis
