Key result
Ypt32p and Mlc1p bind to the Myo2p globular tail domain within the vesicle binding region, consistent with a role in regulating the interaction of post-Golgi carriers with Myo2p subdomain II.
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Elucidates myosin V regulation in yeast; leaves open functional conservation in mammalian vesicle trafficking.
Myosin V is an actin-based motor essential for a variety of cellular processes including skin pigmentation, cell separation and synaptic transmission. Myosin V transports organelles, vesicles and mRNA by binding, directly or indirectly, to cargo-bound receptors via its C-terminal globular tail domain (GTD). We have used the budding yeast myosin V Myo2p to shed light on the mechanism of how Myo2p interacts with post-Golgi carriers. We show that the Rab/Ypt protein Ypt32p, which associates with membranes of the trans-Golgi network, secretory vesicles and endosomes and is related to the mammalian Rab11, interacts with the Myo2p GTD within a region previously identified as the 'vesicle binding region'. Furthermore, we show that the essential myosin light chain 1 (Mlc1p), required for vesicle delivery at the mother-bud neck during cytokinesis, binds to the Myo2p GTD in a region overlapping that of Ypt32p. Our data are consistent with a role of Ypt32p and Mlc1p in regulating the interaction of post-Golgi carriers with Myo2p subdomain II.
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Casavola et al. (2008) studied this question. Ypt32p and Mlc1p bind to the Myo2p globular tail domain within the vesicle binding region, consistent with a role in regulating the interaction of post-Golgi carriers with Myo2p subdomain II.
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