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Publication : MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes.

First Author  El-Amraoui A Year  2002
Journal  EMBO Rep Volume  3
Issue  5 Pages  463-70
PubMed ID  11964381 Mgi Jnum  J:76844
Mgi Id  MGI:2180422 Doi  10.1093/embo-reports/kvf090
Citation  El-Amraoui A, et al. (2002) MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes. EMBO Rep 3(5):463-70
abstractText  Defects of the myosin VIIa motor protein cause deafness and retinal anomalies in humans and mice. We report on the identification of a novel myosin-VIIa-interacting protein that we have named MyRIP (myosin-VIIa- and Rab-interacting protein), since it also binds to Rab27A in a GTP-dependent manner. In the retinal pigment epithelium cells, MyRIP, myosin VIIa and Rab27A are associated with melanosomes. In transfected PC12 cells, overexpression of MyRIP was shown to interfere with the myosin VIIa tail localization. We propose that a molecular complex composed of Rab27A, MyRIP and myosin VIIa bridges retinal melanosomes to the actin cytoskeleton and thereby mediates the local trafficking of these organelles. The defect of this molecular complex is likely to account for the perinuclear mislocalization of the melanosomes observed in the retinal pigment epithelium cells of myosinVIIa-defective mice.
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