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Distinct Rab‐binding domains mediate the interaction of Rabaptin‐5 with GTP‐bound rab4 and rab5
It is reported that native cytosolic Rabaptin‐5 is present in a homodimeric state and dimerization depends upon the presence of its coiled‐coil predicted sequences, and it is proposed that Rabapt in‐between two sequentially acting GTPases to coordinate endocytic and recycling traffic.
The mechanism of internalization of glycosylphosphatidylinositol‐anchored prion protein
It is demonstrated, in primary cultured neurons and the N2a neural cell line, that prion protein is rapidly and constitutively endocytosed, an activity dependent upon its initial basic residues (NH2‐KKRPKP).
Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments
- P. Caswell, May P. Chan, Andrew J. Lindsay, M. Mccaffrey, D. Boettiger, J. Norman
- BiologyThe Journal of cell biology
- 6 October 2008
It is concluded that RCP provides a scaffold that promotes the physical association and coordinate trafficking of α5β1 and EGFR1 and that this drives migration of tumor cells into three-dimensional matrices.
Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport to the endosomal-recycling compartment
- C. Horgan, Sara R. Hanscom, R. Jolly, C. Futter, M. Mccaffrey
- BiologyJournal of Cell Science
- 15 January 2010
It is proposed that FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport of material from peripheral sorting endosomes to the centrally located ERC.
Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments.
Data indicate that Rab25 contributes to tumor progression by directing the localization of integrin-recycling vesicles and thereby enhancing the ability of tumor cells to invade the extracellular matrix.
Rab Coupling Protein (RCP), a Novel Rab4 and Rab11 Effector Protein*
- Andrew J. Lindsay, A. Hendrick, M. Mccaffrey
- Biology, ChemistryThe Journal of Biological Chemistry
- 5 April 2002
Overexpression of the carboxyl-terminal region of RCP, which contains the Rab4- and Rab11-interacting domain, results in a dramatic tubulation of the transferrin compartment, which causes a significant reduction in endosomal recycling.
The dynamic Rab11-FIPs.
A mini-review of the Rab11-FIP field is summarized and the recent findings on FIP function are discussed, at molecular and cellular levels, about the regulation of multiple distinct membrane trafficking events.
Rab25 associates with α5β1 integrin to promote invasive migration in 3D microenvironments
Rab4 affects both recycling and degradative endosomal trafficking
The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane
It is proposed that the C2 domains of the class I Rab11-FIPs function to target these proteins to `docking sites' in the plasma membrane that are enriched in PtdIns(3,4,5)P3 and phosphatidic acid.