Oligomerization activates c-Raf-1 through a Ras-dependent mechanism View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-09

AUTHORS

Zhijun Luo, Guri Tzivion, Peter J. Belshaw, Demetrios Vavvas, Mark Marshall, Joseph Avruch

ABSTRACT

THE c-Raf-1 proto-oncoprotein is a Ras-GTP-regulated protein kinase1 that associates in situ with 14-3-3 proteins2,3, which are naturally dimeric4,5. In COS cells, recombinant Raf is found in oligomeric assemblies. To examine whether induced oligomeriza-tion can alter Raf kinase activity, sequences encoding the FK506-binding protein FKBP12 were fused to the amino terminus of c-Raf-1, introducing a binding site for FK506. Oligomerization of recombinant FKBP-Raf in situ, induced by the addition of the dimeric FK506 derivative FK1012A, activated Raf kinase activity at least half as well as epidermal growth factor (EGF). As with EGF, activation of FKBP-Raf by FK1012A is entirely Ras-GTP dependent. Thus Oligomerization of Raf per se promotes Raf activation through a Ras-dependent mechanism. More... »

PAGES

181-185

Journal

TITLE

Nature

ISSUE

6596

VOLUME

383

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/383181a0

    DOI

    http://dx.doi.org/10.1038/383181a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1044422710

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8774885


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