Literature DB >> 3034679

On the dephosphorylation of the ATP,Mg-dependent protein phosphatase modulator.

J R Vandenheede, C Vanden Abeele, W Merlevede.   

Abstract

The dephosphorylation of the modulator subunit is an essential step in the kinase FA-mediated activation of the ATP,Mg-dependent protein phosphatase. Mg2+ is implicated in this autocatalytic dephosphorylation which is not effected by the addition of phosphoinhibitor-1. Dephosphorylation of free modulator by the catalytic subunit is also largely Mg2+-dependent but can be abolished by phosphoinhibitor-1 in concentrations comparable to the amount of modulator used as substrate (micromolar). The phosphorylase phosphatase activity of the catalytic subunit is inhibited by nanomolar concentrations of phosphoinhibitor-1 and is completely independent of divalent cations.

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Year:  1987        PMID: 3034679     DOI: 10.1016/0014-5793(87)80708-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  Obg-like ATPase 1 regulates global protein serine/threonine phosphorylation in cancer cells by suppressing the GSK3β-inhibitor 2-PP1 positive feedback loop.

Authors:  Dong Xu; Renduo Song; Guohui Wang; Prince V S Jeyabal; Amanda M Weiskoff; Kefeng Ding; Zheng-Zheng Shi
Journal:  Oncotarget       Date:  2016-01-19
  1 in total

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