Direct protein-protein interaction between PLCgamma1 and the bradykinin B2 receptor--importance of growth conditions
| Autor: | Sharmila D. Chauhan, Frédéric Lopez, Jean-Loup Bascands, Jean-Pierre Estève, Joost P. Schanstra, Jean-Pierre Girolami, Christiane Pecher, Johan Duchene |
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| Rok vydání: | 2004 |
| Předmět: |
Receptor
Bradykinin B2 Molecular Sequence Data Biophysics Protein tyrosine phosphatase Biology SH2 domain Biochemistry Structure-Activity Relationship Cricetulus Cricetinae Protein Interaction Mapping Animals Amino Acid Sequence Tyrosine Bradykinin receptor Molecular Biology G protein-coupled receptor Cell Proliferation Binding Sites Phospholipase C Sequence Homology Amino Acid Phospholipase C gamma Cell Biology Surface Plasmon Resonance Molecular biology Type C Phospholipases Phosphorylation Proto-oncogene tyrosine-protein kinase Src Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 326(4) |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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