Different degrees of lever arm rotation control myosin step size

25Citations
Citations of this article
38Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Myosins are actin-based motors that are generally believed to move by amplifying small structural changes in the core motor domain via a lever arm rotation of the light chain binding domain. However, the lack of a quantitative agreement between observed step sizes and the length of the proposed lever arms from different myosins challenges this view. We analyzed the step size of rat myosin 1d (Myo1d) and surprisingly found that this myosin takes unexpectedly large steps in comparison to other myosins. Engineering the length of the light chain binding domain of rat Myo1d resulted in a linear increase of step size in relation to the putative lever arm length, indicative of a lever arm rotation of the light chain binding domain. The extrapolated pivoting point resided in the same region of the rat Myo1d head domain as in conventional myosins. Therefore, rat Myo1d achieves its larger working stroke by a large calculated ∼90° rotation of the light chain binding domain. These results demonstrate that differences in myosin step sizes are not only controlled by lever arm length, but also by substantial differences in the degree of lever arm rotation.

References Powered by Scopus

Tight control of gene expression in mammalian cells by tetracycline- responsive promoters

4407Citations
N/AReaders
Get full text

Three-dimensional structure of myosin subfragment-1: A molecular motor

1942Citations
N/AReaders
Get full text

X-ray Structures of the Myosin Motor Domain of Dictyostelium discoideum Complexed with MgADP.BeF<inf>x</inf> and MgADP.AlF<inf>4</inf><sup>−</sup>

641Citations
N/AReaders
Get full text

Cited by Powered by Scopus

The molecular mechanism of muscle contraction

330Citations
N/AReaders
Get full text

A monomeric myosin VI with a large working stroke

140Citations
N/AReaders
Get full text

Leveraging the membrane - cytoskeleton interface with myosin-1

129Citations
N/AReaders
Get full text

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Cite

CITATION STYLE

APA

Köhler, D., Ruff, C., Meyhöfer, E., & Bähler, M. (2003). Different degrees of lever arm rotation control myosin step size. Journal of Cell Biology, 161(2), 237–241. https://doi.org/10.1083/jcb.200212039

Readers over time

‘11‘12‘13‘14‘15‘16‘17‘18‘19‘20‘21‘22‘23‘2502468

Readers' Seniority

Tooltip

PhD / Post grad / Masters / Doc 12

39%

Researcher 9

29%

Professor / Associate Prof. 7

23%

Lecturer / Post doc 3

10%

Readers' Discipline

Tooltip

Agricultural and Biological Sciences 19

59%

Biochemistry, Genetics and Molecular Bi... 10

31%

Neuroscience 2

6%

Pharmacology, Toxicology and Pharmaceut... 1

3%

Save time finding and organizing research with Mendeley

Sign up for free
0