An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator

被引：85

作者：

Longin, S ^{[1
]}

Jordens, J ^{[1
]}

Martens, E ^{[1
]}

Stevens, I ^{[1
]}

Janssens, V ^{[1
]}

Rondelez, E ^{[1
]}

De Baere, I ^{[1
]}

Derua, R ^{[1
]}

Waelkens, E ^{[1
]}

Goris, J ^{[1
]}

Van Hoof, C ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Faculteit Geneeskunde, Afdeling Biochem, B-3000 Louvain, Belgium

来源：

BIOCHEMICAL JOURNAL | 2004年 / 380卷

关键词：

methylation; methylesterase; phosphorylation; phosphotyrosyl phosphatase activator; protein phosphatase 2A (PP2A); signal transduction;

D O I：

10.1042/BJ20031643

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have described recently the purification and cloning of PP2A (protein phosphatase 2A) leucine carboxylmethyltransferase. We studied the purification of a PP2A-specific methylesterase that co-purifies with PP2A and found that it is tightly associated with an inactive dimeric or trimeric form of PP2A. These inactive enzyme forms could be reactivated as Ser/Thr phosphatase by PTPA ((p) under bar hosphotyrosyl (p) under bar hosphatase (a) under bar ctivator of PP2A). PTPA was described previously by our group as a protein that stimulates the in vitro phosphotyrosyl phosphatase activity of PP2A; how-ever, PP2A-specific methyltransferase could not bring about the activation. The PTPA activation could be distinguished from the Mn2+ stimulation observed with some inactive forms of PP2A, also found associated with PME-1 (phosphatase methylesterase 1). We discuss a potential new function for PME-1 as an enzyme that stabilizes an inactivated pool of PP2A.

引用

页码：111 / 119

页数：9

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