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Real-time Live Imaging of T-cell Signaling Complex Formation
Published on: June 23, 2013
Competition between SLP76 and LAT for PLCγ1 binding in resting T cells
Seung Hee Jung1, Ji Hye Jeong, Hee Jung Seul
1Division of Life and Pharmaceutical Sciences, Ewha Womans University, Seoul, Korea.
European Journal of Immunology
|June 15, 2010
Summary
The constitutive binding of SLP76 to phospholipase Cγ1 (PLCγ1) prevents PLCγ1 from binding to LAT in resting T cells. This interaction is crucial for regulating PLCγ1 membrane recruitment.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- The interaction between SLP76 and PLCγ1 is known.
- The role of this interaction in resting T cells is unclear.
Purpose of the Study:
- To investigate the significance of SLP76-PLCγ1 interaction in resting T cells.
- To determine the molecules associated with PLCγ1 in the absence of SLP76 or its P1 domain.
Main Methods:
- Utilized a mutant Jurkat T-cell line lacking SLP76 or its P1 domain.
- Examined protein associations with PLCγ1 using co-immunoprecipitation and cellular localization studies.
Main Results:
- PLCγ1 associated with LAT when SLP76 binding was blocked.
- This LAT-PLCγ1 association occurred in the cell membrane of resting T cells.
- LAT competed with SLP76 for PLCγ1 binding, mediated by PLCγ1's SH3 domain.
Conclusions:
- Constitutive SLP76-PLCγ1 association prevents LAT binding.
- This interaction also prevents premature PLCγ1 recruitment to the cell membrane.
- SLP76 acts as a negative regulator of PLCγ1 membrane localization in resting T cells.
