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Myotactin, a Novel Hypodermal Protein Involved in Muscle–Cell Adhesion inCaenorhabditis elegans

Myotactin, a Novel Hypodermal Protein Involved in Muscle–Cell Adhesion inCaenorhabditis elegans In C . elegans , assembly of hypodermal hemidesmosome-like structures called fibrous organelles is temporally and spatially coordinated with the assembly of the muscle contractile apparatus, suggesting that signals are exchanged between these cell types to position fibrous organelles correctly. Myotactin, a protein recognized by monoclonal antibody MH46, is a candidate for such a signaling molecule. The antigen, although expressed by hypodermis, first reflects the pattern of muscle elements and only later reflects the pattern of fibrous organelles. Confocal microscopy shows that in adult worms myotactin and fibrous organelles show coincident localization. Further, cell ablation studies show the bodywall muscle cells are necessary for normal myotactin distribution. To investigate myotactin's role in muscle-hypodermal signaling, we characterized the myotactin locus molecularly and genetically. Myotactin is a novel transmembrane protein of ∼500 kd. The extracellular domain contains at least 32 fibronectin type III repeats and the cytoplasmic domain contains unique sequence. In mutants lacking myotactin, muscle cells detach when embryonic muscle contraction begins. Later in development, fibrous organelles become delocalized and are not restricted to regions of the hypodermis previously contacted by muscle. These results suggest myotactin helps maintain the association between the muscle contractile apparatus and hypodermal fibrous organelles. Caenorhabditis elegans cell adhesion cell ablations muscle hemidesmosome-like structures Footnotes 1.used in this paper: FNIII, fibronectin type III; HMM, hidden Markov models Submitted: 12 December 1998 Revision requested 22 June 1999 Accepted: 24 June 1999 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

Myotactin, a Novel Hypodermal Protein Involved in Muscle–Cell Adhesion inCaenorhabditis elegans

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References (59)

Publisher
Rockefeller University Press
Copyright
© 1999 The Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.146.3.659
Publisher site
See Article on Publisher Site

Abstract

In C . elegans , assembly of hypodermal hemidesmosome-like structures called fibrous organelles is temporally and spatially coordinated with the assembly of the muscle contractile apparatus, suggesting that signals are exchanged between these cell types to position fibrous organelles correctly. Myotactin, a protein recognized by monoclonal antibody MH46, is a candidate for such a signaling molecule. The antigen, although expressed by hypodermis, first reflects the pattern of muscle elements and only later reflects the pattern of fibrous organelles. Confocal microscopy shows that in adult worms myotactin and fibrous organelles show coincident localization. Further, cell ablation studies show the bodywall muscle cells are necessary for normal myotactin distribution. To investigate myotactin's role in muscle-hypodermal signaling, we characterized the myotactin locus molecularly and genetically. Myotactin is a novel transmembrane protein of ∼500 kd. The extracellular domain contains at least 32 fibronectin type III repeats and the cytoplasmic domain contains unique sequence. In mutants lacking myotactin, muscle cells detach when embryonic muscle contraction begins. Later in development, fibrous organelles become delocalized and are not restricted to regions of the hypodermis previously contacted by muscle. These results suggest myotactin helps maintain the association between the muscle contractile apparatus and hypodermal fibrous organelles. Caenorhabditis elegans cell adhesion cell ablations muscle hemidesmosome-like structures Footnotes 1.used in this paper: FNIII, fibronectin type III; HMM, hidden Markov models Submitted: 12 December 1998 Revision requested 22 June 1999 Accepted: 24 June 1999

Journal

The Journal of Cell BiologyRockefeller University Press

Published: Aug 9, 1999

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