Next Article in Journal
Improved Prediction of Regulatory Element Using Hybrid Abelian Complexity Features with DNA Sequences
Previous Article in Journal
Delayed Astrogliosis Associated with Reduced M1 Microglia Activation in Matrix Metalloproteinase 12 Knockout Mice during Theiler’s Murine Encephalomyelitis
Previous Article in Special Issue
The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies
Article Menu
Issue 7 (April-1) cover image

Export Article

Open AccessReview

Insights into Actin-Myosin Interactions within Muscle from 3D Electron Microscopy

1
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, USA
2
Department of Cell Biology, Duke University Medical Center, Durham, NC 27607, USA
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(7), 1703; https://doi.org/10.3390/ijms20071703
Received: 6 March 2019 / Revised: 31 March 2019 / Accepted: 1 April 2019 / Published: 5 April 2019
(This article belongs to the Special Issue The Actin-Myosin Interaction in Muscle)
  |  
PDF [10345 KB, uploaded 10 April 2019]
  |  

Abstract

Much has been learned about the interaction between myosin and actin through biochemistry, in vitro motility assays and cryo-electron microscopy (cryoEM) of F-actin, decorated with myosin heads. Comparatively less is known about actin-myosin interactions within the filament lattice of muscle, where myosin heads function as independent force generators and thus most measurements report an average signal from multiple biochemical and mechanical states. All of the 3D imaging by electron microscopy (EM) that has revealed the interplay of the regular array of actin subunits and myosin heads within the filament lattice has been accomplished using the flight muscle of the large water bug Lethocerus sp. The Lethocerus flight muscle possesses a particularly favorable filament arrangement that enables all the myosin cross-bridges contacting the actin filament to be visualized in a thin section. This review covers the history of this effort and the progress toward visualizing the complex set of conformational changes that myosin heads make when binding to actin in several static states, as well as the fast frozen actively contracting muscle. The efforts have revealed a consistent pattern of changes to the myosin head structures as determined by X-ray crystallography needed to explain the structure of the different actomyosin interactions observed in situ. View Full-Text
Keywords: striated muscle; image reconstruction; muscle physiology striated muscle; image reconstruction; muscle physiology
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Taylor, K.A.; Rahmani, H.; Edwards, R.J.; Reedy, M.K. Insights into Actin-Myosin Interactions within Muscle from 3D Electron Microscopy. Int. J. Mol. Sci. 2019, 20, 1703.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top