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Physiology 20: 239-251, 2005; doi:10.1152/physiol.00014.2005
1548-9213/05 $8.00
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Physiology, Vol. 20, No. 4, 239-251, August 2005
© 2005 Int. Union Physiol. Sci./Am. Physiol. Soc.

REVIEW

Myosins: Tails (and Heads) of Functional Diversity

Mira Krendel1 and Mark S. Mooseker1,2,3

1 Departments of Molecular, Cellular, and Developmental Biology;
2 Cell Biology; and
3 Pathology, Yale University, New Haven, Connecticut

mira.krendel{at}yale.edu

The myosin family of actin filament-based molecular motors consists of at least 20 structurally and functionally distinct classes. The human genome contains nearly 40 myosin genes, encoding 12 of these classes. Myosins have been implicated in a variety of intracellular functions, including cell migration and adhesion; intracellular transport and localization of organelles and macromolecules; signal transduction; and tumor suppression. In this review, recent insights into the remarkable diversity in the mechanochemical and functional properties associated with this family of molecular motors are discussed.

* Please note, for uniformity of nomenclature and due to space concerns, myosins are designated by abbreviations (Myo + Arabic numeral denoting myosin class), except in the case of class V budding yeast myosins, which are referred to as Myo2p and Myo4p, and Dictyostelium class I myosins, referred to as MyoA etc., according to accepted nomenclature.




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