Unconventional Myosins in Cell Movement, Membrane Traffic, and Signal Transduction

Author:

Mermall Valerie1,Post Penny L.1,Mooseker Mark S.1

Affiliation:

1. The authors are in the Departments of Biology, Cell Biology, and Pathology, Yale University 342 KBT, New Haven, CT 06520, USA.

Abstract

In the past few years genetic, biochemical, and cytolocalization data have implicated members of the myosin superfamily of actin-based molecular motors in a variety of cellular functions including membrane trafficking, cell movements, and signal transduction. The importance of myosins is illustrated by the identification of myosin genes as targets for disease-causing mutations. The task at hand is to decipher how the multitude of myosins function at both the molecular and cellular level—a task facilitated by our understanding of myosin structure and function in muscle.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference108 articles.

1. We denote myosin classes with roman numerals and refer to specific myosins with arabic numerals.

2. The neck domain is also referred to as the regulatory domain. It consists of one or more 24–amino acid–long IQ (Ile-Gln) motifs that serve as the binding site for myosin light chains. To date only the class XIV Toxoplasma myosin-A lacks a neck region [M. B. Heintzelman and J. D. Schwartzman J. Mol. Biol. 271 139 (1997)].

3. Hasson T., et al., Genomics 36, 431 (1996).

4. Bement W. M., Hasson T., Wirth J. A., Cheney R. E., Mooseker M. S., Proc. Natl. Acad. Sci. U.S.A. 91, 6549 (1994).

5. Spudich J. A., et al., Cold Spring Harbor Symp. Quant. Biol. 60, 783 (1995);

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