Welz, Tobias and Wellbourne-Wood, Joel and Kerkhoff, Eugen (2014) Orchestration of cell surface proteins by Rab11. TRENDS IN CELL BIOLOGY, 24 (7). pp. 407-415. ISSN 0962-8924
Full text not available from this repository. (Request a copy)Abstract
The organization of cells into interconnected structures such as animal tissues requires a sophisticated system directing receptors and adhesion proteins to the cell surface. The Rab11 small G proteins (Rab11a, b, and Rab25) of the Ras superfamily are master regulators of the surface expression of receptors and adhesion proteins. Acting as a molecular switch, Rab11 builds distinct molecular machinery such as motor protein complexes and the exocyst to transport proteins to the cell surface. Recent evidence reveals Rab11 localization at the trans-Golgi network (TGN), post-Golgi vesicles, and the recycling endosome, placing it at the intersection between the endocytic and exocytic trafficking pathways. We review Rab11 in various cellular contexts, and discuss its regulation and mechanisms by which Rab11 couples with effector proteins.
Item Type: | Article |
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Uncontrolled Keywords: | MICROVILLUS INCLUSION DISEASE; FAMILY INTERACTING PROTEIN-2; GTPASE-ACTIVATING PROTEIN; PLASMA-MEMBRANE; EXOCYST COMPLEX; MYOSIN VB; RECYCLING ENDOSOMES; STRUCTURAL BASIS; CYTOPLASMIC DYNEIN; MAMMALIAN-CELLS; Rab11; motor proteins; Rab11-FIP; protruding; Evi5-TBC; Crag-DENN |
Subjects: | 600 Technology > 610 Medical sciences Medicine |
Divisions: | Medicine > Lehrstuhl für Neurologie |
Depositing User: | Petra Gürster |
Date Deposited: | 30 Jul 2020 11:11 |
Last Modified: | 30 Jul 2020 11:16 |
URI: | https://pred.uni-regensburg.de/id/eprint/9974 |
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