Ypt32p and Mlc1p bind within the vesicle binding region of the class V myosin Myo2p globular tail domain.

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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Conserved Sequence, Gene Expression Regulation, Fungal, Molecular Sequence Data, Molecular Structure, Myosin Heavy Chains, Myosin Light Chains, Myosin Type V, Protein Binding, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Secretory Vesicles, Sequence Alignment, Two-Hybrid System Techniques, rab GTP-Binding Proteins
Mol. Microbiol.
Date: Mar. 01, 2008
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