Peer-Reviewed Journal Details
Mandatory Fields
Lindsay, AJ;McCaffrey, MW
2011
April
Journal of Biological Chemistry
Myosin Va Is Required for P Body but Not Stress Granule Formation
Validated
WOS: 14 ()
Optional Fields
CYTOPLASMIC PROCESSING BODIES MESSENGER-RNA TRANSLATION MOTOR PROTEIN COMPLEX TRANSPORT MICROTUBULE CELLS DECAY GENE IDENTIFICATION
286
11519
11528
In the present study we demonstrate an association between mammalian myosin Va and cytoplasmic P bodies, microscopic ribonucleoprotein granules that contain components of the 5'-3' mRNA degradation machinery. Myosin Va colocalizes with several P body markers and its RNAi-mediated knockdown results in the disassembly of P bodies. Overexpression of a dominant-negative mutant of myosin Va reduced the motility of P bodies in living cells. Co-immunoprecipitation experiments demonstrate that myosin Va physically associates with eIF4E, an mRNA binding protein that localizes to P bodies. In contrast, we find that myosin Va does not play a role in stress granule formation. Stress granules are ribonucleoprotein structures that are involved in translational silencing and are spatially, functionally, and compositionally linked to P bodies. Myosin Va is found adjacent to stress granules in stressed cells but displays minimal localization within stress granules, and myosin Va knockdown has no effect on stress granule assembly or disassembly. Combined with recently published reports demonstrating a role for Drosophila and mammalian class V myosins in mRNA transport and the involvement of the yeast myosin V orthologue Myo2p in P body assembly, our results provide further evidence that the class V myosins serve an important role in the transport and turnover of mRNA.
BETHESDA
0021-9258
10.1074/jbc.M110.182808
Grant Details