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MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes
Author(s) -
ElAmraoui Aziz,
Schonn JeanSébastien,
KüsselAndermann Polonca,
Blanchard Stéphane,
Desnos Claire,
Henry JeanPierre,
Wolfrum Uwe,
Darchen François,
Petit Christine
Publication year - 2002
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kvf090
Subject(s) - melanosome , rab , myosin , microbiology and biotechnology , myosin light chain kinase , retinal pigment epithelium , retinal , biology , actin , motor protein , molecular motor , biochemistry , gtpase , microtubule , melanin
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.