Literature DB >> 2306245

TPA stimulates S6 phosphorylation but not protein synthesis in Ehrlich cells.

K S Montine1, E C Henshaw.   

Abstract

Increased phosphorylation of ribosomal protein S6 has been extensively correlated with an increased rate of protein synthesis. We report here that under two separate conditions in Ehrlich cells an increase in the level of S6 phosphorylation does not result in any increase in the rate of protein synthesis. 1) In glutamine-deprived cells TPA stimulates S6 phosphorylation but has no effect on the rate of protein synthesis, 2) In cells deprived of serum growth factors, addition of serum stimulates both S6 phosphorylation and protein synthesis while TPA stimulates only S6 phosphorylation. These results show that increased phosphorylation of S6 is not sufficient to cause increased rates of protein synthesis, and suggest that additional factors may play a more direct role.

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Year:  1990        PMID: 2306245     DOI: 10.1016/0006-291x(90)91013-i

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Antigenic reactivity of ribosomal protein S6 and the calcium-binding ATPase inhibitor protein of mammalian mitochondria.

Authors:  C G Penner; L C Murphy; N J Huzel; E W Yamada
Journal:  Mol Cell Biochem       Date:  1991-11-13       Impact factor: 3.396

2.  The N-terminal region of p27 inhibits HIF-1α protein translation in ribosomal protein S6-dependent manner by regulating PHLPP-Ras-ERK-p90RSK axis.

Authors:  D Zhang; J Liu; X Mi; Y Liang; J Li; C Huang
Journal:  Cell Death Dis       Date:  2014-11-20       Impact factor: 8.469

  2 in total

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