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Gene Review

MYO3  -  myosin 3

Saccharomyces cerevisiae S288c

Synonyms: Actin-dependent myosin-I MYO3, Class I unconventional myosin MYO3, Myosin-3, Type I myosin MYO3, YKL129C
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High impact information on MYO3

  • Deletion of the genes MYO3 and MYO5, which encode the yeast type I myosins, almost abolished growth [1].
  • The yeast type I myosins (MYO3 and MYO5) are involved in endocytosis and in the polarization of the actin cytoskeleton [2].
  • Deletion of MYO3, a yeast gene encoding a "classic" myosin I, has no detectable phenotype [3].
  • We identified CDC50 as a multicopy suppressor of the myo3 myo5-360 temperature-sensitive mutant, which is defective in organization of cortical actin patches [4].
  • Replacement of serine 357 with alanine disrupted the in vivo function of Myo3p, whereas this function was maintained by changing the serine residue to aspartate [5].

Biological context of MYO3


Anatomical context of MYO3

  • Type I myosins in yeast, Myo3p and Myo5p (Myo3/5p), are involved in the reorganization of the actin cytoskeleton [7].
  • Alignment of MYO3 with other unconventional myosins shows that it shares with a subset of them a previously unrecognized region of homology in the tail; this region falls within a domain identified as important for mediating nonspecific electrostatic interactions with membranes [8].

Other interactions of MYO3

  • The budding yeast Saccharomyces cerevisiae has two functionally redundant myosin-I isoforms encoded by the MYO3 and MYO5 genes [5].
  • We have identified and characterized a new adaptor protein, Mti1p (Myosin tail region-interacting protein), which interacts with the SH3 domains of Myo3/5p [7].


  1. Role of type I myosins in receptor-mediated endocytosis in yeast. Geli, M.I., Riezman, H. Science (1996) [Pubmed]
  2. An intact SH3 domain is required for myosin I-induced actin polymerization. Geli, M.I., Lombardi, R., Schmelzl, B., Riezman, H. EMBO J. (2000) [Pubmed]
  3. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. Goodson, H.V., Anderson, B.L., Warrick, H.M., Pon, L.A., Spudich, J.A. J. Cell Biol. (1996) [Pubmed]
  4. Cdc50p, a conserved endosomal membrane protein, controls polarized growth in Saccharomyces cerevisiae. Misu, K., Fujimura-Kamada, K., Ueda, T., Nakano, A., Katoh, H., Tanaka, K. Mol. Biol. Cell (2003) [Pubmed]
  5. The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast. Wu, C., Lytvyn, V., Thomas, D.Y., Leberer, E. J. Biol. Chem. (1997) [Pubmed]
  6. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. Evangelista, M., Klebl, B.M., Tong, A.H., Webb, B.A., Leeuw, T., Leberer, E., Whiteway, M., Thomas, D.Y., Boone, C. J. Cell Biol. (2000) [Pubmed]
  7. The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae. Mochida, J., Yamamoto, T., Fujimura-Kamada, K., Tanaka, K. Genetics (2002) [Pubmed]
  8. Identification and molecular characterization of a yeast myosin I. Goodson, H.V., Spudich, J.A. Cell Motil. Cytoskeleton (1995) [Pubmed]
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