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Titolo:
MOLECULAR-STRUCTURE OF THE SARCOMERIC M-BAND - MAPPING OF TITIN AND MYOSIN BINDING DOMAINS IN MYOMESIN AND THE IDENTIFICATION OF A POTENTIAL REGULATORY PHOSPHORYLATION SITE IN MYOMESIN
Autore:
OBERMANN WMJ; GAUTEL M; WEBER K; FURST DO;
Indirizzi:
MAX PLANCK INST BIOPHYS CHEM,DEPT BIOCHEM,POB 2841 D-37077 GOTTINGEN GERMANY MAX PLANCK INST BIOPHYS CHEM,DEPT BIOCHEM D-37077 GOTTINGEN GERMANY EUROPEAN MOL BIOL LAB,BIOL STRUCT & BIOCOMP PROGRAM D-69012 HEIDELBERG GERMANY UNIV POTSDAM,DEPT CELL BIOL D-14471 POTSDAM GERMANY
Titolo Testata:
EMBO journal
fascicolo: 2, volume: 16, anno: 1997,
pagine: 211 - 220
SICI:
0261-4189(1997)16:2<211:MOTSM->2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
SKELETAL-MUSCLE; M-PROTEIN; PECTORAL MUSCLE; GLOBULAR HEAD; EXPRESSION; SEQUENCES; MOTIFS;
Keywords:
MYOMESIN; MYOSIN BINDING; PHOSPHORYLATION; SARCOMERE; TITIN BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
W.M.J. Obermann et al., "MOLECULAR-STRUCTURE OF THE SARCOMERIC M-BAND - MAPPING OF TITIN AND MYOSIN BINDING DOMAINS IN MYOMESIN AND THE IDENTIFICATION OF A POTENTIAL REGULATORY PHOSPHORYLATION SITE IN MYOMESIN", EMBO journal, 16(2), 1997, pp. 211-220

Abstract

The M band of sarcomeric muscle is a highly complex structure which contributes to the maintenance of the regular lattice of thick filaments. We propose that the spatial coordination of this assembly is regulated by specific interactions of myosin filaments, the M band protein myomesin and the large carboxy-terminal region of titin, Corresponding binding sites between these proteins were identified, Myomesin binds myosin in the central region of light meromyosin (LMM, myosin residues 1506-1674) by its unique aminoterminal domain My1. A single titin immunoglobulin domain, m4, interacts with a myomesin fragment spanning domains My4-My6. This interaction is regulated by phosphorylation of Ser482 in the linker between myomesin domains My4 and My5. Myomesin phosphorylation at this site by cAMP-dependent kinase and similar or identical activities in muscle extracts block the association with titin. We propose that this demonstration of a phosphorylation-controlled interaction in the sarcomeric cytoskeleton is of potential relevance for sarcomere formation and/or turnover, It also reveals how binding affinities of modular proteins can be regulated by modifications of inter-domain linkers.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:42:06