α-subunit of farnesyltransferase is phosphorylated in vivo

Effect of protein phosphatase-1 on enzymatic activity

Amit Kumar, Maureen H. Beresini, Punita Dhawan, Kamal D. Mehta

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Farnesyltransferase is a heterodimer consisting of a 49 kDa α-subunit and a 46 kDa β-subunit. In this report, we demonstrate that the endogenous heterodimeric farnesyltransferase protein is phosphorylated at the α-subunit in vivo and phosphorylation plays a role in the regulation of farnesyltransferase activity. In vivo 32P-labeling of PC-12 cells followed by immunoprecipitation with specific anti rat α-subunit IgG showed a labeled α-subunit protein band at an expected molecular mass of 49 kDa. Treatment of PC-12 cells with protein phosphatase inhibitor, Calyculin A, resulted in a decrease in FTase activity, and phophoserine/phosphothreonine-specific protein phosphatase-1 treatment of PC-12 and GM37 cell extracts resulted in 100% and 375% increase in farnesyltransferase activity, respectively, compared to untreated extracts.

Original languageEnglish (US)
Pages (from-to)445-452
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume222
Issue number2
DOIs
StatePublished - May 15 1996

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Farnesyltranstransferase
Protein Phosphatase 1
Phosphothreonine
Phosphorylation
Phosphoprotein Phosphatases
Protein Subunits
Molecular mass
Cell Extracts
Immunoprecipitation
Labeling
Rats
Immunoglobulin G

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

α-subunit of farnesyltransferase is phosphorylated in vivo : Effect of protein phosphatase-1 on enzymatic activity. / Kumar, Amit; Beresini, Maureen H.; Dhawan, Punita; Mehta, Kamal D.

In: Biochemical and Biophysical Research Communications, Vol. 222, No. 2, 15.05.1996, p. 445-452.

Research output: Contribution to journalArticle

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