The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo.

Détails

ID Serval
serval:BIB_9B9F9545BA28
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo.
Périodique
Journal of Biological Chemistry
Auteur(s)
Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
06/1994
Peer-reviewed
Oui
Volume
269
Numéro
23
Pages
16311-16317
Langue
anglais
Notes
Publication types: Comparative Study ; Journal Article
Résumé
We have used polyclonal antibodies against an internal peptide (residues 169 to 182; Ab169/182) and a peptide corresponding to the carboxyl terminus (residues 299 to 309; Ab299/309) to look for in vivo modifications of protein phosphatase 2A catalytic (PP2Ac) subunit. Treatment of extracts from human breast cancer (MCF7) cells with either alkali or ethanol increased immunoreactivity of PP2Ac subunit severalfold on Western blots with Ab299/309, but did not apparently change molecular weight or isoelectric point of the protein. In contrast, immunoreactivity with Ab169/182 was unchanged by these treatments. Subsequently, we demonstrated that the increase in PP2Ac subunit recognition by Ab299/309 coincides with the demethylation of this protein at the carboxyl-terminal leucine (Leu309). Methylation of PP2Ac subunit, in vitro, increases its activity toward both phosphorylase a and a phosphopeptide. The carboxyl-terminal sequence (TPDYFL) of PP2Ac subunit is completely conserved between mammals, yeast, fruit fly, and plants which suggests that regulation of this enzyme activity by carboxyl-terminal methylation has been conserved during evolution.
Mots-clé
Amino Acid Sequence, Breast Neoplasms, Catalysis, Conserved Sequence, Female, Humans, Leucine/analogs & derivatives, Methylation, Molecular Sequence Data, Oligopeptides/chemistry, Oligopeptides/metabolism, Phosphoprotein Phosphatases/chemistry, Phosphoprotein Phosphatases/immunology, Phosphorylase a/metabolism, Phosphorylation, Protein Methyltransferases/metabolism, Protein Phosphatase 2, Protein Processing, Post-Translational, Sequence Homology, Amino Acid, Structure-Activity Relationship, Tumor Cells, Cultured
Pubmed
Web of science
Création de la notice
25/01/2008 17:32
Dernière modification de la notice
20/08/2019 16:02
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