A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex.

Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followed by an acidic domain. ...
The myosin-I SH3 domain interacted with both Bee1p and Vrp1p, yeast homologues of human WASP and WIP, adapter proteins that link actin assembly and signaling molecules. The myosin-I acidic domain interacted with Arp2/3 complex subunits, Arc40p and Arc19p, and showed both sequence similarity and genetic redundancy with the COOH-terminal acidic domain of Bee1p (Las17p), which controls Arp2/3-mediated actin nucleation. These findings suggest that myosin-I proteins may participate in a diverse set of motility functions through a role in actin assembly.
Mesh Terms:
Actin-Related Protein 2, Actin-Related Protein 3, Actins, Amino Acid Sequence, Cell Movement, Cytoskeletal Proteins, Fungal Proteins, Ligands, Microfilament Proteins, Models, Biological, Molecular Motor Proteins, Molecular Sequence Data, Morphogenesis, Myosin Heavy Chains, Myosin Type I, Myosins, Protein Binding, Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Wiskott-Aldrich Syndrome Protein
J. Cell Biol.
Date: Jan. 24, 2000
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