Raf kinases mediate the phosphorylation of eukaryotic translation elongation factor 1A and regulate its stability in eukaryotic cells

URN to cite this document:: urn:nbn:de:bvb:355-epub-305747
DOI to cite this document:: 10.5283/epub.30574

Sanges, C. ; Scheuermann, C. ; Zahedi, R. P. ; Sickmann, A. ; Lamberti, A. ; Migliaccio, N. ; Baljuls, A. ; Marra, M. ; Zappavigna, S. ; Reinders, Jörg ; Rapp, U. ; Abbruzzese, A. ; Caraglia, M. ; Arcari, P.

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Date of publication of this fulltext: 08 Aug 2014 09:32

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Abstract

We identified eukaryotic translation elongation factor 1A (eEF1A) Raf-mediated phosphorylation sites and defined their role in the regulation of eEF1A half-life and of apoptosis of human cancer cells. Mass spectrometry identified in vitro S21 and T88 as phosphorylation sites mediated by B-Raf but not C-Raf on eEF1A1 whereas S21 was phosphorylated on eEF1A2 by both B- and C-Raf. Interestingly, S21 ...