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Titolo:
STRUCTURAL BASIS FOR ACTIVATION OF THE TITIN KINASE DOMAIN DURING MYOFIBRILLOGENESIS
Autore:
MAYANS O; VANDERVEN PFM; WILM M; MUES A; YOUNG P; FURST DO; WILMANNS M; GAUTEL M;
Indirizzi:
DESY,EUROPEAN MOL BIOL LAB,HAMBURG OUTSTN,NOTKESTR 85 D-22603 HAMBURGGERMANY DESY,EUROPEAN MOL BIOL LAB,HAMBURG OUTSTN D-22603 HAMBURG GERMANY UNIV POTSDAM,DEPT CELL BIOL D-14471 POTSDAM GERMANY EUROPEAN MOL BIOL LAB D-69012 HEIDELBERG GERMANY
Titolo Testata:
Nature
fascicolo: 6705, volume: 395, anno: 1998,
pagine: 863 - 869
SICI:
0028-0836(1998)395:6705<863:SBFAOT>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
GIANT PROTEIN-KINASES; CRYSTAL-STRUCTURE; INSULIN-RECEPTOR; TYROSINE KINASE; IMMUNOELECTRON MICROSCOPY; MOLLUSCAN TWITCHIN; PEPTIDE SUBSTRATE; PHOSPHORYLATION; EXPRESSION; MUSCLE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
O. Mayans et al., "STRUCTURAL BASIS FOR ACTIVATION OF THE TITIN KINASE DOMAIN DURING MYOFIBRILLOGENESIS", Nature, 395(6705), 1998, pp. 863-869

Abstract

The giant muscle protein titin (connectin) is essential in the temporal and spatial control of the assembly of the highly ordered sarcomeres (contractile units) of striated muscle. Here we present the crystal structure of titin's only catalytic: domain, an autoregulated serine kinase (titin kinase). The structure shows how the active site is inhibited by a tyrosine of the kinase domain. We describe a dual mechanism of activation of titin kinase that consists of phosphorylation of thistyrosine and binding of calcium/calmodulin to the regulatory tail. The serine kinase domain of titin is the first known non-arginine-aspartate kinase to be activated by phosphorylation. The phosphorylated tyrosine is not located in the activation segment, as in other kinases, but in the P + 1 loop, indicating that this tyrosine is a binding partner of the titin kinase substrate. Titin kinase phosphorylates the muscle protein telethonin in early differentiating myocytes, indicating that this kinase may act in myofibrillogenesis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 14:02:48