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Adenosine diphosphate and strain sensitivity in myosin motors

Nyitrai, Miklos, Geeves, Michael A. (2004) Adenosine diphosphate and strain sensitivity in myosin motors. Philosophical Transactions of the Royal Society B: Biological Sciences, 359 (1452). pp. 1867-77. ISSN 0962-8436. (doi:10.1098/rstb.2004.1560) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:13203)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
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The release of adenosine diphosphate (ADP) from the actomyosin cross-bridge plays an important role in the adenosine-triphosphate-driven cross-bridge cycle. In fast contracting muscle fibres, the rate at which ADP is released from the cross-bridge correlates with the maximum shortening velocity of the muscle fibre, and in some models the rate of ADP release defines the maximum shortening velocity. In addition, it has long been thought that the rate of ADP release could be sensitive to the load on the cross-bridge and thereby provide a molecular explanation of the Fenn effect. However, direct evidence of a strain-sensitive ADP-release mechanism has been hard to come by for fast muscle myosins. The recently published evidence for a strain-sensing mechanism involving ADP release for slower muscle myosins, and in particular non-muscle myosins, is more compelling and can provide the mechanism of processivity for motors such as myosin V. It is therefore timely to examine the evidence for this strain-sensing mechanism. The evidence presented here will argue that a strain-sensitive mechanism of ADP release is universal for all myosins but the basic mechanism has evolved in different ways for different types of myosin. Furthermore, this strain-sensing mechanism provides a way of coordinating the action of multiple myosin motor domains in a single myosin molecule, or in complex assemblies of myosins over long distances without invoking a classic direct allosteric or cooperative communication between motors.

Item Type: Article
DOI/Identification number: 10.1098/rstb.2004.1560
Additional information: 0962-8436 (Print) Journal Article Review
Uncontrolled keywords: Actins/metabolism/*physiology Adenosine Diphosphate/metabolism/*physiology Animals *Models, Biological Molecular Motors/*physiology Muscle Contraction/*physiology Muscle, Skeletal/*physiology Myosins/metabolism/*physiology Research Support, Non-U.S. Gov't
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Michael Geeves
Date Deposited: 29 May 2009 06:19 UTC
Last Modified: 16 Nov 2021 09:51 UTC
Resource URI: (The current URI for this page, for reference purposes)
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