Myosins Are Motor Proteins of the Actomyosin Motility System: Association with Membranes and with the Signal Pathways

Myosins Are Motor Proteins of the Actomyosin Motility System: Association with Membranes and with... Structural and functional characteristics of the motor proteins of the actomyosin motility system, myosins, which can be grouped into 15 classes, are presented in brief. The structure of the myosin molecule is considered: a conservative motor domain of the head with ATP- and actin-binding sites, a head segment associated with light chains, and a tail, which is variable in various myosins performing different functions. We address the progress in the studies of myosin functioning as a motor in the in vitroassay systems. Not only animal and prokaryotic organisms but also Characean algae and plant pollen tubes contributed considerably to these studies as sources of actin and myosin. Higher-plant myosins are characterized. The data are presented concerning the interaction between some myosin forms and other actin-binding proteins and, on the other hand, the phosphoinositol signal transduction pathway, the integral plasmalemmal proteins, and the proteins of the extracellular matrix. The most important idea formulated in the review is that a dynamic reorganization of the actin cytoskeleton is a structural basis for physiological processes in plants. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Myosins Are Motor Proteins of the Actomyosin Motility System: Association with Membranes and with the Signal Pathways

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Publisher
Kluwer Academic Publishers-Plenum Publishers
Copyright
Copyright © 2001 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1023/A:1016728607442
Publisher site
See Article on Publisher Site

Abstract

Structural and functional characteristics of the motor proteins of the actomyosin motility system, myosins, which can be grouped into 15 classes, are presented in brief. The structure of the myosin molecule is considered: a conservative motor domain of the head with ATP- and actin-binding sites, a head segment associated with light chains, and a tail, which is variable in various myosins performing different functions. We address the progress in the studies of myosin functioning as a motor in the in vitroassay systems. Not only animal and prokaryotic organisms but also Characean algae and plant pollen tubes contributed considerably to these studies as sources of actin and myosin. Higher-plant myosins are characterized. The data are presented concerning the interaction between some myosin forms and other actin-binding proteins and, on the other hand, the phosphoinositol signal transduction pathway, the integral plasmalemmal proteins, and the proteins of the extracellular matrix. The most important idea formulated in the review is that a dynamic reorganization of the actin cytoskeleton is a structural basis for physiological processes in plants.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Oct 10, 2004

References

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