Activity of protein phosphatases against initiation factor-2 and elongation factor-2

N. T. Redpath, Christopher Proud

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

The protein phosphatases active against phosphorylase a, elongation factor-2 (EF-2) and the α-subunit of initiation factor-2 (eIF-2) [eIF-2(αP)] were studied in extracts of rabbit reticulocytes, Swiss-mouse 3T3 fibroblasts and rat hepatocytes, by use of the specific phosphatase inhibitors okadaic acid and inhibitor proteins-1 and -2. In all three extracts tested, both phosphatase-1 and phosphatase-2A contributed to overall phosphatase activity against phosphorylase and eIF-2(αP), but phosphatases-2B and -2C did not. In contrast, only protein phosphatase-2A was active against EF-2. Furthermore, in hepatocytes there was substantial type-2C phosphatase activity against EF-2, but not against phosphorylase or eIF-2α. These findings in cell extracts were borne out by data obtained by studying the activities of purified protein phosphatase-1 and -2A against eIF-2(αP) and EF-2. eIF-2(αP) was a moderately good substrate for both enzymes (relative to phosphorylase a). In contrast, EF-2 was a very poor substrate for protein phosphatase-1, but was dephosphorylated faster than phosphorylase a by protein phosphatase-2A. The implications of these findings for the control of translation and their relationships to previous work are discussed.

LanguageEnglish
Pages175-180
Number of pages6
JournalBiochemical Journal
Volume272
Issue number1
DOIs
Publication statusPublished - 1 Jan 1990

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "The protein phosphatases active against phosphorylase a, elongation factor-2 (EF-2) and the α-subunit of initiation factor-2 (eIF-2) [eIF-2(αP)] were studied in extracts of rabbit reticulocytes, Swiss-mouse 3T3 fibroblasts and rat hepatocytes, by use of the specific phosphatase inhibitors okadaic acid and inhibitor proteins-1 and -2. In all three extracts tested, both phosphatase-1 and phosphatase-2A contributed to overall phosphatase activity against phosphorylase and eIF-2(αP), but phosphatases-2B and -2C did not. In contrast, only protein phosphatase-2A was active against EF-2. Furthermore, in hepatocytes there was substantial type-2C phosphatase activity against EF-2, but not against phosphorylase or eIF-2α. These findings in cell extracts were borne out by data obtained by studying the activities of purified protein phosphatase-1 and -2A against eIF-2(αP) and EF-2. eIF-2(αP) was a moderately good substrate for both enzymes (relative to phosphorylase a). In contrast, EF-2 was a very poor substrate for protein phosphatase-1, but was dephosphorylated faster than phosphorylase a by protein phosphatase-2A. The implications of these findings for the control of translation and their relationships to previous work are discussed.",
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Activity of protein phosphatases against initiation factor-2 and elongation factor-2. / Redpath, N. T.; Proud, Christopher.

In: Biochemical Journal, Vol. 272, No. 1, 01.01.1990, p. 175-180.

Research output: Contribution to journalArticle

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