Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3.

Roland JT, Kenworthy AK, Peranen J, Caplan S, Goldenring JR
Mol Biol Cell. 2007 18 (8): 2828-37

PMID: 17507647 · PMCID: PMC1949367 · DOI:10.1091/mbc.e07-02-0169

Cells use multiple pathways to internalize and recycle cell surface components. Although Rab11a and Myosin Vb are involved in the recycling of proteins internalized by clathrin-mediated endocytosis, Rab8a has been implicated in nonclathrin-dependent endocytosis and recycling. By yeast two-hybrid assays, we have now demonstrated that Myosin Vb can interact with Rab8a, but not Rab8b. We have confirmed the interaction of Myosin Vb with Rab11a and Rab8a in vivo by using fluorescent resonant energy transfer techniques. Rab8a and Myosin Vb colocalize to a tubular network containing EHD1 and EHD3, which does not contain Rab11a. Myosin Vb tail can cause the accumulation of both Rab11a and Rab8a in collapsed membrane cisternae, whereas dominant-negative Rab11-FIP2(129-512) selectively accumulates Rab11a but not Rab8a. Additionally, dynamic live cell imaging demonstrates distinct pathways for Rab11a and Rab8a vesicle trafficking. These findings indicate that Rab8a and Rab11a define different recycling pathways that both use Myosin Vb.

MeSH Terms (15)

Animals Carrier Proteins Chickens Fluorescence Resonance Energy Transfer HeLa Cells Histocompatibility Antigens Class I Humans Myosin Type V Protein Binding Protein Transport Rabbits rab GTP-Binding Proteins Transport Vesicles Two-Hybrid System Techniques Vesicular Transport Proteins

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