Direct protein-protein interaction between PLCgamma1 and the bradykinin B2 receptor--importance of growth conditions.
Biochem Biophys Res Commun
; 326(4): 894-900, 2005 Jan 28.
Article
em En
| MEDLINE
| ID: mdl-15607753
ABSTRACT
Recently, we have described a novel protein-protein interaction between the G-protein coupled bradykinin B2 receptor and tyrosine phosphatase SHP-2 via an immunoreceptor tyrosine-based inhibition motif (ITIM) sequence located in the C-terminal part of the B2 receptor and the Src homology (SH2) domains of SHP-2. Here we show that phospholipase C (PLC)gamma1, another SH2 domain containing protein, can also interact with this ITIM sequence. Using surface plasmon resonance analysis, we observed that PLCgamma1 interacted with a peptide containing the phosphorylated form of the bradykinin B2 receptor ITIM sequence. In CHO cells expressing the wild-type B2 receptor, bradykinin-induced transient recruitment and activation of PLCgamma1. Interestingly, this interaction was only observed in quiescent and not in proliferating cells. Mutation of the key ITIM residue abolished this interaction with and activation of PLCgamma1. Finally we also identified bradykinin-induced PLCgamma1 recruitment and activation in primary culture renal mesangial cells.
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Bases de dados:
MEDLINE
Assunto principal:
Fosfolipases Tipo C
/
Mapeamento de Interação de Proteínas
/
Receptor B2 da Bradicinina
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
França