Identification of Nck interacting proteins in vascular smooth muscle cells.
作者： Udo Schmitz , Kerstin Thömmes , Imke Beier , Rainer Düsing , Hans Vetter
关键词: Signal transducing adaptor protein 、 Immunoprecipitation 、 Tyrosine 、 Biology 、 Kinase 、 Phosphorylation 、 Angiotensin II 、 Dynamin 、 Cell biology 、 Biochemistry 、 Signal transduction
摘要: The adaptor molecule Nck has been demonstrated to mediate Angiotensin II (AngII)-induced stimulation of p21-activated kinase (PAK) and c-Jun NH2-terminal (JNK) in vascular smooth muscle cells (VSMC). We have previously demonstrated, that immunoprecipitation from VSMC stimulated by AngII yielded an unidentified 100 kD phosphotyrosine (pTyr) protein. present study was aimed at identifying the Nck-associated pTyr protein VSMC. Several candidate proteins appropriate size, had shown either bind or implicated signal transduction pathways leading activation PAK JNK were tested for association with first we Git1, which did not upon AngII. However, identified dynamin as a bound VSCM via interaction third Nck-SH3 domain. tyrosine phosphorylated treatment seemed be distinct found immunoprecipitates. Future work will now identify functional studies address its role signaling.
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