JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 3 May 2002. doi:10.1083/jcb1574iti5
This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dove, A. W.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Dove, A. W.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
© The Rockefeller University Press, 0021-9525/2002/5/545-b $5.00
The Journal of Cell Biology, Volume 157, Number 4, May 13, 2002 545-b-545

In This Issue

 A muscular job for spectrin
Worms lacking {alpha}-spectrin (right) do not elongate.

All multicellular animals examined have a spectrin cytoskeleton, suggesting that it serves some important, although so far poorly understood, function. On page 665, Norman and Moerman provide significant new insights into spectrin activity in C. elegans, where the tetrameric molecule seems to be required for normal development of body wall muscle and muscle attachment structures.

The authors identified and characterized spc-1, the only {alpha} spectrin gene in C. elegans. Localization of {alpha} spectrin to the cell membrane during development requires ß spectrin, but not ßHeavy spectrin. A null mutation in spc-1 blocks complete elongation of the worm embryo, which dies shortly after hatching. Elongation appears to be required for normal muscle development, and worms with mutations in spectrin genes develop a disorganized apical actin cytoskeleton in the hypodermis and broad muscle cells with misshapen myofilaments.

Surprisingly, the absence of spectrin does not appear to cause the broad muscle cell shape directly. Instead, the absence of spectrin in the hypodermis interferes with microfilament stability, which in turn interferes with the early elongation of the embryo. Broad muscle cells are a result of this failure in elongation. The authors' new genetic system should facilitate further dissection of complex interactions between tissues during development. {blacksquare}



Alan W. Dove

alanwdove{at}earthlink.net


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?

Related Article

{alpha} spectrin is essential for morphogenesis and body wall muscle formation in Caenorhabditis elegans
Kenneth R. Norman and Donald G. Moerman
J. Cell Biol. 2002 157: 665-677. [Abstract] [Full Text] [PDF]




This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dove, A. W.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Dove, A. W.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents