Molecular Structure of Sarcomere-to-Membrane Attachment at M-Lines in C. elegans Muscle

• Type of Material: Article
• Authors: Hiroshi Qadota, Emory University; Guy Benian, Emory University
• Language: English
• Date: 2010-04-19
• Publisher: Hindawi Publishing Corporation
• Publication Version: Final Published Version
• Copyright Statement: © 2010 H. Qadota and G. M. Benian.
• License: Creative Commons Attribution 3.0 Unported
• Final Published Version (URL): http://www.hindawi.com/journals/bmri/2010/864749/
• Title of Journal or Parent Work: Journal of Biomedicine and Biotechnology
• ISSN: 1110-7243
• Volume: 2010
• Issue: 2010
• Start Page: 1
• End Page: 9
• Grant/Funding Information: The authors wish to thank support for their studies from Grants nos. AR052133 and AR051466 from the National Institutes of Health.
• Research Categories: Health Sciences, Pathology; Biology, Cell

Abstract

C. elegans is an excellent model for studying nonmuscle cell focal adhesions and the analogous muscle cell attachment structures. In the major striated muscle of this nematode, all of the M-lines and the Z-disk analogs (dense bodies) are attached to the muscle cell membrane and underlying extracellular matrix. Accumulating at these sites are many proteins associated with integrin. We have found that nematode M-lines contain a set of protein complexes that link integrin-associated proteins to myosin thick filaments. We have also obtained evidence for intriguing additional functions for these muscle cell attachment proteins.