Link to Pubmed [PMID] – 10889203
Link to HAL – hal-04161691
Link to DOI – 10.1074/jbc.M004393200
Journal of Biological Chemistry, 2000, 275 (38), pp.29654-29659. ⟨10.1074/jbc.M004393200⟩
To gain an insight into the cellular function of the unconventional myosin VIIA, we sought proteins interacting with its tail region, using the yeast two-hybrid system. Here we report on one of the five candidate interactors we identified, namely the type Iα regulatory subunit (RIα) of protein kinase A. The interaction of RIα with myosin VIIA tail was demonstrated by coimmunoprecipitation from transfected HEK293 cells. Analysis of deleted constructs in the yeast two-hybrid system showed that the interaction of myosin VIIA with RIα involves the dimerization domain of RIα. In vitrobinding assays identified the C-terminal “4.1, ezrin, radixin, moesin” (FERM)-like domain of myosin VIIA as the interacting domain. In humans and mice, mutations in the myosin VIIAgene underlie hereditary hearing loss, which may or may not be associated with visual deficiency. Immunohistofluorescence revealed that myosin VIIA and RIα are coexpressed in the outer hair cells of the cochlea and rod photoreceptor cells of the retina. Our results strongly suggest that myosin VIIA is a novel protein kinase A-anchoring protein that targets protein kinase A to definite subcellular sites of these sensory cells.