A conserved role for myosin VII in adhesion.
The class VII myosins (M7) are expressed in a wide range of organisms. M7 mutants in mice, zebrafish and Dictyostelium exhibit phenotypes that reveal a role for M7 in adhesion in these highly divergent systems, suggesting a basic conservation of M7 function throughout evolution. M7s are characterized by the presence of two FERM domains in their C-terminal tail region, and deletion of either from the Dictyostelium M7 (DdM7) tail results in loss of function without affecting localization. A search for DdM7 binding partners has revealed that talin, an actin-binding protein that provides a key link between adhesion receptors and the actin cytoskeleton, interacts directly with DdM7. The phenotypes of the DdM7 and talin null mutants are highly similar, suggesting that these two proteins work co-operatively to maintain cell-cell and cell-surface contact and that this interaction may also be conserved throughout evolution.
Titus
Margaret A
MA
Department of Genetics, Cell Biology & Development, University of Minnesota, Minneapolis 55455, USA.
D000818:Animals; D002448:Cell Adhesion; D004398:Dyneins / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D000081412:Myosin VIIa; D009218:Myosins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D015800:Protozoan Proteins / Q000737:chemistry / Q000378:metabolism; D016608:Talin / Q000737:chemistry / Q000378:metabolism
C000631455:MYO7A protein, human; C000631456:Myo7a protein, mouse; D000081412:Myosin VIIa; D015800:Protozoan Proteins; D016608:Talin; C407348:myosin VII protein, Dictyostelium discoideum; D009218:Myosins; D004398:Dyneins