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- W2155102198 abstract "Vertebrate-striated muscle is assumed to owe its remarkable order to the molecular ruler functions of the giant modular signaling proteins, titin and nebulin. 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 ∼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 of obscurin 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 become detectable 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." @default.
- W2155102198 created "2016-06-24" @default.
- W2155102198 creator A5049291585 @default.
- W2155102198 creator A5060131441 @default.
- W2155102198 creator A5062353668 @default.
- W2155102198 date "2001-07-09" @default.
- W2155102198 modified "2023-10-14" @default.
- W2155102198 title "Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly" @default.
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- W2155102198 doi "https://doi.org/10.1083/jcb.200102110" @default.
- W2155102198 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2196875" @default.
- W2155102198 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11448995" @default.
- W2155102198 hasPublicationYear "2001" @default.
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