Recruitment of PLC-gamma1 to SLP-76

Stable Identifier
Reaction [binding]
Homo sapiens
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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.

Literature References
PubMed ID Title Journal Year
11390650 Identification of a phospholipase C-gamma1 (PLC-gamma1) SH3 domain-binding site in SLP-76 required for T-cell receptor-mediated activation of PLC-gamma1 and NFAT

Yablonski, D, Kadlecek, T, Weiss, A

Mol Cell Biol 2001
11048639 The mechanism of phospholipase C-gamma1 regulation

Kim, MJ, Kim, E, Ryu, SH, Suh, PG

Exp Mol Med 2000
Orthologous Events
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