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A metal-dependent form of protein phosphatase 2A.

Abstract：

:Highly purified bovine heart protein phosphatase 2A catalytic subunit lost virtually all of its activity during storage at -70 degrees. When the enzyme was preincubated with Co2+, over 35% of the original activity was restored. Freshly prepared protein phosphatase 2A purified from bovine heart was stimulated at least 3 to 4-fold by pretreatment with Co2+ or Mn2+. Activation by Co2+ appeared to be irreversible whereas activation by Mn2+ was partially reversed after the cation was chelated with excess EDTA/EGTA. The sensitivity of Co2(+)-stimulated protein phosphatase 2A to okadaic acid or inhibitor-2 was similar to that of spontaneously active protein phosphatase 2A. The enzyme was converted to a latent form by treatment with phosphate or pyrophosphate. The latent form was completely reactivated by preincubation with Co2+. These results demonstrate that protein phosphatase 2A, like phosphatase 1, can exist in a metal ion-dependent form and may represent a new mechanism for the regulation of protein phosphatase 2A activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Cai L,Chu Y,Wilson SE,Schlender KK

doi

10.1006/bbrc.1995.1334

subject

Has Abstract

pub_date

1995-03-08 00:00:00

pages

274-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X85713344

journal_volume

208

pub_type

杂志文章

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