Key result
Overexpression of myosin 1b or addition of cytochalasin D affects the morphology of sorting multivesicular endosomes and delays the processing of Pmel17 in the human pigmented MNT-1 cell line.
Myosin 1b controls the traffic of protein cargo in multivesicular endosomes by modulating their morphology with actin.
No immediate clinical implications from cell-line data; leaves open myosin 1b's role in pigmentation disorders for in vivo validation.
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.
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Salas‐Cortés et al. (2005) studied this question. Overexpression of myosin 1b or addition of cytochalasin D was evaluated on Morphology of sorting multivesicular endosomes and processing of Pmel17. Overexpression of myosin 1b or addition of cytochalasin D affects the morphology of sorting multivesicular endosomes and delays the processing of Pmel17 in the human pigmented MNT-1 cell line.
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