Journal Article

PUBDB-2017-09675

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural basis for activation of the titin kinase domain during myofibrillogenesis.

Mayans, O.Extern* ; van der Ven, P. F. ; Wilm, M. ; Mues, A. ; Young, P. ; Fürst, D. O. ; Wilmanns, M.DESY* ; Gautel, M.

1998
Nature Publ. Group London [u.a.]

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Please use a persistent id in citations: doi:10.1038/27603

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 this tyrosine 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.

Keyword(s): Connectin ; Muscle Proteins ; Protein Kinase Inhibitors ; Recombinant Proteins ; TCAP protein, human ; TTN protein, human ; Tyrosine ; Protein Kinases

Note: F-Bereich; EMBL

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Contributing Institute(s):

1. DESY Retrocat (DESY(-2012))

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Experiment(s):

1. No specific instrument

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; BIOSIS Previews ; Current Contents - Agriculture, Biology and Environmental Sciences ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 30 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record

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