Direct protein-protein interaction between PLCgamma1 and the bradykinin B2 receptor--importance of growth conditions |
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Authors: | Duchene Johan Chauhan Sharmila D Lopez Frédéric Pecher Christiane Estève Jean-Pierre Girolami Jean-Pierre Bascands Jean-Loup Schanstra Joost P |
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Affiliation: | Inserm U388, IFR 31, Hopital Rangueil, TSA 50032, 31059 Toulouse Cedex 9, France. |
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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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Keywords: | G-protein coupled receptor Bradykinin B2 receptor Protein-protein interaction Phospholipase Cγ1 Tyrosine phosphatase SHP-2 Src homology 2 domain Surface plasmon resonance Mesangial cells Quiescent and proliferating conditions |
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