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Competition between SLP76 and LAT for PLCγ1 binding in resting T cells

Title
Competition between SLP76 and LAT for PLCγ1 binding in resting T cells
Authors
Jung S.H.Jeong J.H.Seul H.J.Lee J.R.
Ewha Authors
이종란
SCOPUS Author ID
이종란scopus
Issue Date
2010
Journal Title
European Journal of Immunology
ISSN
0014-2980JCR Link
Citation
vol. 40, no. 8, pp. 2330 - 2339
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The constitutive interaction between the P1 domain (a 67-amino-acid functional domain within the proline-rich region) of SLP76 and the SH3 domain of phospholipase Cγ1 (PLCγ1) has been shown. To determine the significance of the interaction between SLP76 and PLCγ1 in resting T cells, we examined molecules associated with PLCγ1 in the absence of both SLP76 and, more specifically, the P1 domain of SLP76. Using a mutant Jurkat T-cell line, we showed that PLCγ1 associated with LAT when the constitutive association with SLP76 was blocked. We also found that the PLCγ1 association with LAT occurred in the membranes of resting T cells. Further experiments demonstrated that LAT competed with SLP76 for PLCγ1 binding and that the LAT interaction with PLCγ1 was mediated by the SH3 domain of PLCγ1. Collectively, these results suggest that the constitutive association of SLP76 with PLCγ1 is required to prevent the association with LAT as well as the premature recruitment of PLCγ1 to the cell membrane. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
DOI
10.1002/eji.200939411
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자연과학대학 > 생명과학전공 > Journal papers
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