Complex formation between RAS and RAF and other protein kinases.

作者：Linda Van Aelst, Maureen M. Barr, S Marcus, Anthony J. Polverino, Michael H. Wigler · 发表于：Proceedings of the National Academy of Sciences · 年份：1993 · DOI：10.1073/pnas.90.13.6213 · 被引用次数：644 · 研究领域：Protein Kinase Regulation and GTPase Signaling、Melanoma and MAPK Pathways、Ubiquitin and proteasome pathways

We used a Saccharomyces cerevisiae genetic system to detect the physical interaction of RAS and RAF oncoproteins. We also observed interaction between RAS and byr2, a protein kinase implicated as a mediator of the Schizosaccharomyces pombe ras1 protein. Interaction with RAS required only the N-terminal domains of RAF or byr2 and was disrupted by mutations in either the guanine nucleotide-binding or effector-loop domains of RAS. We observed interaction between MEK (a kinase that phosphorylates mitogen-activated protein kinases) and the catalytic domain of RAF. RAS and MEK also interacted but only when RAF was overexpressed.