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First published online October 11, 2005
doi: 10.1242/10.1242/jcs.02607

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Myosin Ib modulates the morphology and the protein transport within multi-vesicular sorting endosomes

Laura Salas-Cortes^1,*, Fei Ye^2,*, Danièle Tenza¹, Claire Wilhelm³, Alexander Theos⁴, Daniel Louvard¹, Graça Raposo¹ and Evelyne Coudrier^1,

¹ Institut Curie, CNRS UMR144, 26 rue d'Ulm, 75248, Paris, Cedex 05, France
² E363 INSERM, Faculté de Médecine, Necker, 156 Rue de Vaugirard, 75015, Paris, France
³ Laboratoire des milieux désordonnés et hétérogènes, Universite Pierre et Marie Curie, Boite 86, 4 Place Jussieu, 75252 Paris Cedex 05, France
⁴ Department of Pathology and Laboratory Medicine, University of Pennsylvania, 3451 Walnut Street, Philadelphia, PA 19104, USA

Author for correspondence (e-mail: coudrier{at}curie.fr)

Accepted 2 August 2005

Members of at least four classes of myosin (I, II, V and VI) have been implicated in the dynamics of a large variety of organelles. Despite their common motor domain structure, some of these myosins, however, are non processive and cannot move organelles along the actin tracks. Here, we demonstrate in the human pigmented MNT-1 cell line that, (1) the overexpression of one of these myosins, myosin 1b, or the addition of cytochalasin D affects the morphology of the sorting multivesicular endosomes; (2) the overexpression of myosin 1b delays the processing of Pmel17 (the product of murine silver locus also named GP100), which occurs in these multivesicular endosomes; (3) myosin 1b associated with endosomes coimmunoprecipitates with Pmel17. All together, these observations suggest that myosin 1b controls the traffic of protein cargo in multivesicular endosomes most probably through its ability to modulate with actin the morphology of these sorting endosomes.

Key words: Actin cytoskeleton, Biogenesis of melanosomes, Membrane traffic, Endocytosis

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