Novel interaction partners of the TPR/MET tyrosine kinase

• Published in: The FASEB journal Vol. 19; no. 2; pp. 267 - 269
• Main Authors: Schaaf, Christian P, Benzing, Jörg, Schmitt, Thomas, Erz, Dorothee H. R, Tewes, Magdalena, Bartram, Claus R, Janssen, Johannes W. G
• Format: Journal Article
• Language: English
• Published: United States 01.02.2005
• Subjects: Animals; Blotting, Western - methods; Embryo, Mammalian - chemistry; Embryo, Mammalian - metabolism; Gene Library; Humans; Kidney - cytology; Kidney - embryology; Mice; Mutagenesis, Site-Directed - genetics; Oncogene Proteins, Fusion - chemistry; Oncogene Proteins, Fusion - metabolism; Peptides; Protein Binding; Protein Interaction Mapping - methods; Proto-Oncogene Proteins - chemistry; Proto-Oncogene Proteins - metabolism; Proto-Oncogene Proteins c-met; Rats; Receptors, Growth Factor - chemistry; Receptors, Growth Factor - metabolism; Sequence Analysis, Protein - methods; Substrate Specificity; Two-Hybrid System Techniques
• ISSN: 0892-6638; 1530-6860
• DOI: 10.1096/fj.04-1558fje

A large variety of biological processes is mediated by stimulation of the receptor tyrosine kinase MET. Screening a mouse embryo cDNA library, we were able to identify several novel, putative intracellular TPR/MET-substrates: SNAPIN, DCOHM, VAV-1, Sorting nexin 2, Death associated protein kinase 3, SMC-1, Centromeric protein C, and hTID-1. Interactions as identified by yeast two-hybrid analysis were validated in vitro and in vivo by mammalian two-hybrid studies, a far-western assay and coimmunoprecipitation. Participation in apoptosis-regulating mechanisms through interaction with DAPK-3 and cell cycle control via binding to nuclear proteins such as CENPC and SMC-1 are possible new aspects of intracellular MET signaling.