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      Orchestration of cell surface proteins by Rab11.

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          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.

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          Author and article information

          Journal
          Trends Cell Biol.
          Trends in cell biology
          1879-3088
          0962-8924
          Jul 2014
          : 24
          : 7
          Affiliations
          [1 ] Molecular Cell Biology Laboratory, Department of Neurology, University Hospital Regensburg, Franz-Josef-Strauss Allee 11, Regensburg, Germany.
          [2 ] Molecular Cell Biology Laboratory, Department of Neurology, University Hospital Regensburg, Franz-Josef-Strauss Allee 11, Regensburg, Germany. Electronic address: eugen.kerkhoff@klinik.uni-regensburg.de.
          Article
          S0962-8924(14)00033-6
          10.1016/j.tcb.2014.02.004
          24675420
          4249d3bf-a916-450e-9946-dea5fb51f647
          Copyright © 2014 Elsevier Ltd. All rights reserved.
          History

          Crag-DENN,Evi5-TBC,Rab11,Rab11-FIP,motor proteins,protruding
          Crag-DENN, Evi5-TBC, Rab11, Rab11-FIP, motor proteins, protruding

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