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Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases
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SYSNO ASEP 0023676 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases Title IIntramolekulární regulace ZAP-70: analogie s receptorovými tyrosin kinasami Author(s) Brdička, Tomáš (UMG-J) RID
Kadlecek, T.A. (US)
Roose, J.P. (US)
Pastuszak, A.W. (US)
Weiss, A. (US)Source Title Molecular and Cellular Biology. - : American Society for Microbiology - ISSN 0270-7306
Roč. 25, č. 12 (2005), s. 4924-4933Number of pages 10 s. Language eng - English Country US - United States Keywords protein tyrosin-kinase ; phosphorylation ; ZAP-70 Subject RIV EB - Genetics ; Molecular Biology CEZ AV0Z50520514 - UMG-J (2005-2011) Annotation ZAP-70 is a cytoplasmic tyrosine kinase required to couple the activated T cell antigen receptor to downstream signaling pathways. It contains two tandem SH2 domains separated from a C-terminal catalytic domain by the region termed Interdomain B. Interdomain B has striking regulatory effects on ZAP-70 function, but its deletion leads only to minor defects. To resolve this paradox we utilized the analogy with several receptor tyrosine kinases (RTK) which are in the resting state autoinhibited by the interaction between their kinase domain and tyrosine residues within their juxtamembrane region. Autoinhibition is released when these tyrosines become phosphorylated following receptor stimulation. Based on mutagenesis analysis we found that Interdomain B downregulates ZAP-70 catalytic activity in a similar manner as the juxtamembrane region of RTKs. This finding suggests that a general autoinhibitory mechanism employed by RTKs is also used by some cytoplasmic tyrosine-kinases. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2006
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