Orchestration of cell surface proteins by Rab11

• The vesicle transport protein Rab11 has diverse cellular functions and its dysregulation is linked to cancer.
• Rab11 proteins form complexes with myosin, kinesin, and dynein motor proteins.
• The GTP/GDP status of Rab11 allows for distinct protein complex formation.
• TBC and DENN family proteins regulate the Rab11 GTP/GDP cycle.

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.