Source:http://www.reactome.org/biopax/48887BiochemicalReaction2271
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Authored: Rudd, C.E., de Bono, B, Garapati, P V, 2008-01-24 15:53:10,
PLC-gamma1 plays an important role in transducing the external signal in to second messengers by hydrolysing PIP2. PLC-gamma1 contains an N-term PH domain, a catalytic domain 'X' followed by two SH2 domains and an SH3 domain, a C-term catalytic domain 'Y' and a C2 domain (Ca++ binding). PLC-gamma1 interacts with both SLP-76 aswell as LAT. It interacts with its SH3 domain to the proline rich sequence of SLP-76. This interaction aids in localizing PLC-gamma1 to the membrane. This recruitment of PLC-gamma1 to LAT and SLP-76 is essential for its TCR induced tyrosine phosphorylation and activation.,
Reviewed: Trowsdale, J, 2008-02-26 12:02:59
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Recruitment of PLC-gamma1 to SLP-76
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