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Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization.

Publication ,  Journal Article
Lechler, T; Shevchenko, A; Li, R
Published in: J Cell Biol
January 24, 2000

The generation of cortical actin filaments is necessary for processes such as cell motility and cell polarization. Several recent studies have demonstrated that Wiskott-Aldrich syndrome protein (WASP) family proteins and the actin-related protein (Arp) 2/3 complex are key factors in the nucleation of actin filaments in diverse eukaryotic organisms. To identify other factors involved in this process, we have isolated proteins that bind to Bee1p/Las17p, the yeast WASP-like protein, by affinity chromatography and mass spectroscopic analysis. The yeast type I myosins, Myo3p and Myo5p, have both been identified as Bee1p-interacting proteins. Like Bee1p, these myosins are essential for cortical actin assembly as assayed by in vitro reconstitution of actin nucleation sites in permeabilized yeast cells. Analysis using this assay further demonstrated that the motor activity of these myosins is required for the polymerization step, and that actin polymerization depends on phosphorylation of myosin motor domain by p21-activated kinases (PAKs), downstream effectors of the small guanosine triphosphatase, Cdc42p. The type I myosins also interact with the Arp2/3 complex through a sequence at the end of the tail domain homologous to the Arp2/3-activating region of WASP-like proteins. Combined deletions of the Arp2/3-interacting domains of Bee1p and the type I myosins abolish actin nucleation sites at the cortex, suggesting that these proteins function redundantly in the activation of the Arp2/3 complex.

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Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

January 24, 2000

Volume

148

Issue

2

Start / End Page

363 / 373

Location

United States

Related Subject Headings

  • cdc42 GTP-Binding Protein
  • Wiskott-Aldrich Syndrome Protein
  • Schizosaccharomyces pombe Proteins
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Proteins
  • Protein Binding
  • Phosphorylation
  • Myosins
  • Myosin Type V
 

Citation

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Lechler, T., Shevchenko, A., & Li, R. (2000). Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J Cell Biol, 148(2), 363–373. https://doi.org/10.1083/jcb.148.2.363
Lechler, T., A. Shevchenko, and R. Li. “Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization.J Cell Biol 148, no. 2 (January 24, 2000): 363–73. https://doi.org/10.1083/jcb.148.2.363.
Lechler T, Shevchenko A, Li R. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J Cell Biol. 2000 Jan 24;148(2):363–73.
Lechler, T., et al. “Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization.J Cell Biol, vol. 148, no. 2, Jan. 2000, pp. 363–73. Pubmed, doi:10.1083/jcb.148.2.363.
Lechler T, Shevchenko A, Li R. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J Cell Biol. 2000 Jan 24;148(2):363–373.

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

January 24, 2000

Volume

148

Issue

2

Start / End Page

363 / 373

Location

United States

Related Subject Headings

  • cdc42 GTP-Binding Protein
  • Wiskott-Aldrich Syndrome Protein
  • Schizosaccharomyces pombe Proteins
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Proteins
  • Protein Binding
  • Phosphorylation
  • Myosins
  • Myosin Type V