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Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases
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SYSNO ASEP 0023676 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Ostatní články Název Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases Překlad názvu IIntramolekulární regulace ZAP-70: analogie s receptorovými tyrosin kinasami Tvůrce(i) Brdička, Tomáš (UMG-J) RID
Kadlecek, T.A. (US)
Roose, J.P. (US)
Pastuszak, A.W. (US)
Weiss, A. (US)Zdroj.dok. Molecular and Cellular Biology. - : American Society for Microbiology - ISSN 0270-7306
Roč. 25, č. 12 (2005), s. 4924-4933Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova protein tyrosin-kinase ; phosphorylation ; ZAP-70 Vědní obor RIV EB - Genetika a molekulární biologie CEZ AV0Z50520514 - UMG-J (2005-2011) Anotace 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. Pracoviště Ústav molekulární genetiky Kontakt Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Rok sběru 2006
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