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Titolo:
Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
Autore:
Young, P; Ehler, E; Gautel, M;
Indirizzi:
Max Planck Inst Mol Physiol, Dept Phys Biochem, D-44202 Dortmund, Germany Max Planck Inst Mol Physiol Dortmund Germany D-44202 2 Dortmund, Germany European Mol Biol Lab, Struct Biol Div, D-69117 Heidelberg, Germany European Mol Biol Lab Heidelberg Germany D-69117 117 Heidelberg, Germany ETH Honggerberg, Inst Cell Biol, CH-8093 Zurich, Switzerland ETH Honggerberg Zurich Switzerland CH-8093 , CH-8093 Zurich, Switzerland
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 1, volume: 154, anno: 2001,
pagine: 123 - 136
SICI:
0021-9525(20010709)154:1<123:OAGSRG>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
SKELETAL-MUSCLE CELLS; M-LINE; KINASE DOMAIN; Z-DISK; MONOCLONAL-ANTIBODIES; MOLECULAR-STRUCTURE; THICK FILAMENTS; MAP KINASE; I-BAND; TITIN;
Keywords:
obscurin; Rho GTPases; GEF proteins; myofibril; heart muscle;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
75
Recensione:
Indirizzi per estratti:
Indirizzo: Gautel, M Max Planck Inst Mol Physiol, Dept Phys Biochem, Postfach 500 247, D-44202 Dortmund, Germany Max Planck Inst Mol Physiol Postfach 500 247 Dortmund Germany D-44202
Citazione:
P. Young et al., "Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly", J CELL BIOL, 154(1), 2001, pp. 123-136

Abstract

Vertebrate-striated muscle is assumed to owe its remarkable order to the molecular ruler functions of the giant modular signaling proteins, titin andnebulin. It was believed that these two proteins represented unique results of protein evolution in vertebrate muscle. In this paper we report the identification of a third giant protein from vertebrate muscle, obscurin, encoded on chromosome 1q42. Obscurin is similar to 800 kD and is expressed specifically in skeletal and cardiac muscle. The complete cDNA sequence of obscurin reveals a modular architecture, consisting of >67 intracellular immunoglobulin (Ig)- or fibronectin-3-like domains with multiple splice variants. A large region of obscurin shows a modular architecture of tandem Ig domains reminiscent of the elastic region of titin. The COOH-terminal region ofobscurin interacts via two specific Ig-like domains with the NH2-terminal Z-disk region of titin. Both proteins coassemble during myofibrillogenesis. During the progression of myofibrillogenesis, all obscurin epitopes becomedetectable at the M band. The presence of a calmodulin-binding IQ motif, and a Rho guanine nucleotide exchange factor domain in the COOH-terminal region suggest that obscurin is involved in Ca2+/calmodulin, as well as G protein-coupled signal transduction in the sarcomere.

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Documento generato il 26/11/20 alle ore 20:04:36