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Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments
Here we show that blocking the adhesive function of αvβ3 integrin with soluble RGD ligands, such as osteopontin or cilengitide, promoted association of Rab-coupling protein (RCP) with α5β1 integrinExpand
The mechanism of internalization of glycosylphosphatidylinositol‐anchored prion protein
The mode of internalization of glycosylphosphatidylinositol‐anchored proteins, lacking any cytoplasmic domain by which to engage adaptors to recruit them into coated pits, is problematical; that ofExpand
Distinct Rab‐binding domains mediate the interaction of Rabaptin‐5 with GTP‐bound rab4 and rab5
Rabaptin‐5 functions as an effector for the small GTPase Rab5, a regulator of endocytosis and early endosome fusion. We have searched for structural determinants that confer functional specificity onExpand
Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport to the endosomal-recycling compartment
Several protein families control intracellular transport processes in eukaryotic cells. Here, we show that the Rab11 GTPase effector protein Rab11-FIP3 (henceforth, FIP3) directly interacts with theExpand
Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments.
Here, we report a direct interaction between the beta1 integrin cytoplasmic tail and Rab25, a GTPase that has been linked to tumor aggressiveness and metastasis. Rab25 promotes a mode of migration onExpand
Rab Coupling Protein (RCP), a Novel Rab4 and Rab11 Effector Protein*
Rab4 and Rab11 are small GTPases belonging to the Ras superfamily. They both function as regulators along the receptor recycling pathway. We have identified a novel 80-kDa protein that interactsExpand
The dynamic Rab11-FIPs.
The Rab11-FIPs (Rab11-family interacting proteins; also known as FIPs) constitute an evolutionarily conserved protein family that act as effector molecules for multiple Rab and Arf (ADP-ribosylationExpand
Rab25 associates with α5β1 integrin to promote invasive migration in 3D microenvironments
Here, we report a direct interaction between the beta1 integrin cytoplasmic tail and Rab25, a GTPase that has been linked to tumor aggressiveness and metastasis. Rab25 promotes a mode of migration onExpand
Rab4 affects both recycling and degradative endosomal trafficking
The small GTPases Rab4, Rab5 and Rab7 are endosomal proteins which play important roles in the regulation of various stages of endosomal trafficking. Rab4 and Rab5 have both been localized to earlyExpand
Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis.
The Rab11-family interacting protein 3 (Rab11-FIP3), also known as Arfophilin and Eferin, is a Rab11 and ADP-ribosylation factor (ARF) binding protein of unknown function. Here, we sought toExpand
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