PuSH - Publikationsserver des Helmholtz Zentrums München: Protein kinase Cα activates RAF-1 by direct phosphorylation.

Informationen

Hinweise zu Qualitätskriterien von Zeitschriften

Open-Access-Richtlinie der Helmholtz-Gemeinschaft 2016

CC Licencences

Metriken für Publikationen

Navigation

Startseite

English

Recherche

Erweiterte Suche

Durchblättern nach ...

... HMGU-Autoren/Konsortien

... Organisationsstruktur

... Zeitschriften

... Publikationstypen

... Forschungsdaten

... Arbeitsgruppen

... Erscheinungsjahr

Publikationen im Überblick

Statistik

HGF Fortschrittsbericht

OA Publikationen

Eintragen

Neue Publikation eintragen

Neue Publikation holen aus...

...EVA

Fehlende Publikation melden

Highlights

Suche

Hilfe & Kontakt

Ansprechpartner

Hilfe

Datenschutz

Helmholtz Open Science

Bibliometrische Indikatoren

SHERPA/RoMEO

DOAJ

Export:

Text

Endnote (RIS) BIB

BibTeX

Kolch, W. ; Heldecker, G.* ; Kochs, G.G.* ; Hummel, R.* ; Vahidi, H.* ; Mischak, H.* ; Finkenzeller, G.* ; Marmé, D.* ; Rapp, U.R.*

Protein kinase Cα activates RAF-1 by direct phosphorylation.

Nature 364, 249-252 (1993)

DOI

PMC

Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.

Abstract
Metriken
Zusatzinfos

THE kinase Raf-1 can be activated by treatment of cells with mitogens and by the protein kinase C (PKC) activator 12-O-tetradecanoyl-phorbol-13-acetate (TPA) (reviewed in refs 1, 2). Activated Raf-1 triggers a protein kinase cascade by direct phosphorylation of MAP kinase kinase3-5, resulting in phosphorylation of ternary complex factor6 and Jun7,8 by MAP kinase. Here we investigate the molecular mechanism and biological consequences of PKCα-mediated Raf-1 activation in NIH3T3 fibroblasts. PKCα directly phosphorylates and activates Raf-1 both in vitro and in vivo. PKCα induces Raf-1 phosphorylation at several sites, including a serine residue at position 499. Mutation of serine at this position or at residue 259 does not abrogate Raf-1 stimulation by a combination of Ras plus the src tyrosine kinase Lck, but severely impedes Raf-1 activation by PKCα. Consistent with such a direct interaction is the observation that Raf-1 and PKCα cooperate in the transformation of NIH3T3 cells. The Ser499 phosphorylation site is necessary for this synergism.

Impact Factor

Scopus SNIP

Scopus
Cited By

Altmetric

0.000

8.822

1122