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Article

A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity.

Nature - 2 Jul 1998

Tzivion G, Luo Z, Avruch J

Abstract excerpt

cRaf-1 is a mitogen-activated protein kinase that is the main effector recruited by GTP-bound Ras in order to activate the MAP kinase pathway. Inactive Raf is found in the cytosol in a complex with Hsp90, Hsp50 (Cdc37) and the 14-3-3 proteins. GTP-bound Ras binds Raf and is necessary but not sufficient for the stable activation of Raf that occurs in response to serum, epidermal growth factor, platelet-derived...

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Identifiers

PMID: 9665134
DOI: 10.1038/27938

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity.PMID 9665134Read ↗

Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association.Semantic proximity Read ↗

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New insights into Raf regulation from structural analyses.Semantic proximity Read ↗

The C-terminus of Raf-1 acts as a 14-3-3-dependent activation switch.Semantic proximity Read ↗

B-Raf autoinhibition in the presence and absence of 14-3-3.Semantic proximity Read ↗

Disruption of the 14-3-3 binding site within the B-Raf kinase domain uncouples catalytic activity from PC12 cell differentiation.Semantic proximity Read ↗

14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner.Semantic proximity Read ↗

Ras-Raf complexes in vitro.Semantic proximity Read ↗

Mutational activation of c-raf-1 and definition of the minimal transforming sequence.Semantic proximity Read ↗

CRAF autophosphorylation of serine 621 is required to prevent its proteasome-mediated degradation.Semantic proximity Read ↗

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