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

Seung Hee Jung, Ji Hye Jeong, Hee Jung Seul, Jong Ran Lee

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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.

Original languageEnglish
Pages (from-to)2330-2339
Number of pages10
JournalEuropean Journal of Immunology
Volume40
Issue number8
DOIs
StatePublished - Aug 2010

Keywords

  • LAT
  • Phospholipase Cγ1
  • Signalling
  • SSLP76
  • T cell

Fingerprint

Dive into the research topics of 'Competition between SLP76 and LAT for PLCγ1 binding in resting T cells'. Together they form a unique fingerprint.

Cite this