Physiol Rev Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Physiol. Rev. 85: 1001-1060, 2005; doi:10.1152/physrev.00019.2004
0031-9333/05 $18.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow A corrigendum has been published
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (5)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hooper, S. L.
Right arrow Articles by Thuma, J. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hooper, S. L.
Right arrow Articles by Thuma, J. B.

Invertebrate Muscles: Muscle Specific Genes and Proteins

Scott L. Hooper and Jeffrey B. Thuma

Neuroscience Program, Department of Biological Sciences, Ohio University, Athens, Ohio

This is the first of a projected series of canonic reviews covering all invertebrate muscle literature prior to 2005 and covers muscle genes and proteins except those involved in excitation-contraction coupling (e.g., the ryanodine receptor) and those forming ligand- and voltage-dependent channels. Two themes are of primary importance. The first is the evolutionary antiquity of muscle proteins. Actin, myosin, and tropomyosin (at least, the presence of other muscle proteins in these organisms has not been examined) exist in muscle-like cells in Radiata, and almost all muscle proteins are present across Bilateria, implying that the first Bilaterian had a complete, or near-complete, complement of present-day muscle proteins. The second is the extraordinary diversity of protein isoforms and genetic mechanisms for producing them. This rich diversity suggests that studying invertebrate muscle proteins and genes can be usefully applied to resolve phylogenetic relationships and to understand protein assembly coevolution. Fully achieving these goals, however, will require examination of a much broader range of species than has been heretofore performed.


Address for reprint requests and other correspondence: Address for reprint requests and other correspondence: S. L. Hooper, Neuroscience Program, Dept. of Biological Sciences, Irvine Hall, Ohio University, Athens, OH 45701 (E-mail: hooper{at}ohio.edu)




This article has been cited by other articles:


Home page
J. Cell Sci.Home page
L. Fabian, X. Xia, D. V. Venkitaramani, K. M. Johansen, J. Johansen, D. J. Andrew, and A. Forer
Titin in insect spermatocyte spindle fibers associates with microtubules, actin, myosin and the matrix proteins skeletor, megator and chromator
J. Cell Sci., July 1, 2007; 120(13): 2190 - 2204.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
A. A. Hopitzan, A. J. Baines, and E. Kordeli
Molecular Evolution of Ankyrin: Gain of Function in Vertebrates by Acquisition of an Obscurin/Titin-Binding-Related Domain
Mol. Biol. Evol., January 1, 2006; 23(1): 46 - 55.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2005 by the American Physiological Society.