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I-mediated signaling events by Lyn kinase C-terminal tyrosine phosphorylation
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SYSNO ASEP 0109003 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title I-mediated signaling events by Lyn kinase C-terminal tyrosine phosphorylation Title Pozitivní a negativní regulace signalizačních dějů zprostředkovaných Fcepsilon receptorem I pomocí fosforylace C-koncového tyrozinu kinázy Lyn Author(s) Tolar, Pavel (UMG-J)
Dráberová, Lubica (UMG-J) RID
Tolarová, Helena (UMG-J)
Dráber, Petr (UMG-J) RIDSource Title European Journal of Immunology. - : Wiley - ISSN 0014-2980
Roč. 34, č. 4 (2004), s. 1136-1145Number of pages 10 s. Language eng - English Country DE - Germany Keywords mast cell ; Fc receptor ; signal transduction Subject RIV EB - Genetics ; Molecular Biology R&D Projects LN00A026 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA204/00/0204 GA ČR - Czech Science Foundation (CSF) GA310/00/0205 GA ČR - Czech Science Foundation (CSF) GA204/03/0594 GA ČR - Czech Science Foundation (CSF) GA301/03/0596 GA ČR - Czech Science Foundation (CSF) IAA5052005 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) IAA7052006 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) IAA5052310 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z5052915 - UMG-J Annotation Using a phospho-Lyn-specific antiserum, we show an increased phosphorylation of the Lyn C-terminal regulatory tyrosine and decreased Lyn kinase activity during Fc epsilon RI-mediated mast cell activation. Mutant Lyn, defective in the C-terminal tyrosine, constitutively phosphorylated several substrates in resting cells, but did not cause Fc epsilon RI internalization or spontaneous degranulation. Fc epsilon RI-induced signaling in the presence of constitutively active Lyn exhibited enhanced phosphorylation of the receptor subunits, Syk, LAT, Gab2, phospholipase C (PLC)gamma 1 and PLC gamma 2, and production of phosphatidylinositol 3,4,5-trisphosphate. Although enzymatic activities of PLC gamma 1 and PLC gamma 2 were also up-regulated, amounts of inositol 1,4,5-trisphosphate, mobilization of intracellular calcium and degranulation were suppressed. Additionally, constitutively active Lyn was strikingly less efficient than wild-type Lyn in restoring the receptor-mediated calcium responses in bone marrow mast cells derived from Lyn(-/-) mice. These findings pinpoint the tight regulation of Lyn kinase activity as a critical event in mast cell degranulation Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2005
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