The ubiquitination of ribosomal S6 kinases is independent from the mitogen-induced phosphorylation/activation of the kinase

International Journal of Biochemistry and Cell Biology

Volumn 41, Issue 4, 2009, Pages 828-833

  Gwalter, J ^a   Wang, M L ^a   Gout, I ^a,b  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b INSTITUTE OF MOLECULAR BIOLOGY AND GENETICS   (Ukraine)

Author keywords

Mitogenic stimulation; Phosphorylation activation; S6 kinases; Stresses; Ubiquitination

Indexed keywords

GROWTH FACTOR; MITOGENIC AGENT; PROTEASOME; S6 KINASE; STAUROSPORINE;

ARTICLE; CELL GROWTH; CELL STRAIN HEK293; ENERGY METABOLISM; ENZYME ACTIVATION; ENZYME ASSAY; ENZYME LOCALIZATION; ENZYME REGULATION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MITOGENESIS; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; RIBOSOME; SERUM; SIGNAL TRANSDUCTION; UBIQUITINATION; ULTRAVIOLET RADIATION;

CELL LINE; ENZYME ACTIVATION; HUMANS; ISOENZYMES; PHOSPHORYLATION; PROTEIN ISOFORMS; RIBOSOMAL PROTEIN S6 KINASES; SIGNAL TRANSDUCTION; STAUROSPORINE; TRANSFECTION; UBIQUITIN; UBIQUITINATION; ULTRAVIOLET RAYS;

EID: 59649097612     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.08.018     Document Type: Article

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