Tarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back-Reference-Cited by-同舟云学术

Tarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back

Published:2015 Issue:8 Volume:11 Page:2180-2189
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Alamo Lorenzo¹²³⁴,Li Xiaochuan (Edward)⁵⁶⁷⁸,Espinoza-Fonseca L. Michel⁹¹⁰¹¹¹²⁸,Pinto Antonio¹²³⁴,Thomas David D.⁹¹⁰¹¹¹²⁸,Lehman William⁵⁶⁷⁸,Padrón Raúl¹²³⁴^ORCID

Affiliation:

1. Centro de Biología Estructural

2. Instituto Venezolano de Investigaciones Científicas (IVIC)

3. Caracas 1020

4. Venezuela

5. Department of Physiology and Biophysics

6. Boston University School

7. Boston

8. USA

9. Department of Biochemistry

10. Molecular Biology and Biophysics

11. University of Minnesota

12. Minneapolis

Abstract

Tarantula thick filament activation stiffens myosin regulatory light chain N-terminal extension by sequential phosphorylation hindering the docking back of the free head.

Funder

American Heart Association

National Institutes of Health

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2015/MB/C5MB00163C

Reference45 articles.

1. Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom.

2. A. Szent-Györgyi , Regulatory Mechanisms of Striated Muscle Contraction, Springer, Japan, 2007, vol. 592, pp. 253–264