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PMID: 2812002 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans.

Nature ·Vol. 342 ·No. 6245 ·1989-11-02 ·Pages 45-50

Benian GM, Kiff JE, Neckelmann N, Moerman DG, Waterston RH

Abstract

The Caenorhabditis elegans gene unc-22 encodes a very large muscle protein, called twitchin, which consists of a protein kinase domain and several copies of two short motifs. The sequence of twitchin has unexpected similarities to the sequences of proteins of the immunoglobulin superfamily, cell adhesion molecules and vertebrate muscle proteins, including myosin light-chain kinase. These homologies, together with results from earlier genetic and molecular analyses, indicate that twitchin is involved in a novel mechanism of myosin regulation.

MeSH Terms
Amino Acid Sequence Animals Caenorhabditis/genetics,metabolism Caenorhabditis elegans Proteins Calmodulin-Binding Proteins Genes Helminth Proteins/genetics Molecular Sequence Data Muscle Proteins/genetics Myosin-Light-Chain Kinase/genetics Myosins/metabolism Protein Kinases/genetics Restriction Mapping Sequence Homology, Nucleic Acid
Chemicals
Caenorhabditis elegans Proteins Calmodulin-Binding Proteins Helminth Proteins Muscle Proteins unc-22 protein, C elegans Protein Kinases Myosin-Light-Chain Kinase Myosins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Benian G M
Department of Pathology, Emory University School of Medicine, Atlanta, Georgia 30322.
Kiff J E
Neckelmann N
Moerman D G
Waterston R H
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1989-11-02
Pages
45-50
Language
English
Region
England
NLM ID
0410462
Subset
IM
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