Jenny Schafer
Last active: 6/12/2017

Rab11-FIP2 interaction with MYO5B regulates movement of Rab11a-containing recycling vesicles.

Schafer JC, Baetz NW, Lapierre LA, McRae RE, Roland JT, Goldenring JR
Traffic. 2014 15 (3): 292-308

PMID: 24372966 · PMCID: PMC4081500 · DOI:10.1111/tra.12146

A tripartite association of Rab11a with both Rab11-FIP2 and MYO5B regulates recycling endosome trafficking. We sought to define the intermolecular interactions required between Rab11-FIP2 and MYO5B. Using a random mutagenesis strategy, we identified point mutations at S229P or G233E in Rab11-FIP2 that caused loss of interaction with MYO5B in yeast two-hybrid assays as well as loss of interaction of Rab11-FIP2(129-356) with MYO5B tail when expressed in HeLa cells. Single mutations or the double S229P/G233E mutation failed to alter the association of full-length Rab11-FIP2 with MYO5B tail in HeLa cells. While EGFP-Rab11-FIP2 wild type colocalized with endogenous MYO5B staining in MDCK cells, EGFP-Rab11-FIP2(S229P/G233E) showed a significant decrease in localization with endogenous MYO5B. Analysis of Rab11a-containing vesicle movement in live HeLa cells demonstrated that when the MYO5B/Rab11-FIP2 association is perturbed by mutation or by Rab11-FIP2 knockdown, vesicle movement is increased in both speed and track length, consistent with an impairment of MYO5B tethering at the cytoskeleton. These results support a critical role for the interaction of MYO5B with Rab11-FIP2 in stabilizing the functional complex with Rab11a, which regulates dynamic movements of membrane recycling vesicles.

© 2013 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.

MeSH Terms (15)

Animals Binding Sites Carrier Proteins Dogs Endosomes HeLa Cells Humans Madin Darby Canine Kidney Cells Membrane Proteins Myosin Heavy Chains Myosin Type V Point Mutation Protein Binding Protein Transport rab GTP-Binding Proteins

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