Interaction of nucleoredoxin with protein phosphatase 2A

详细信息    查看全文

• 作者：Katarzyna Lechward ; Ewa Sugajska ; Ivo de Baere ; Jozef Goris ; Brian A. Hemmings and Stanislaw Zolnierowicz
• 关键词：Reversible phosphorylation ; Protein– ; protein interaction ; Protein phosphatase type 2A ; Redox regulation
• 刊名：FEBS Letters
• 出版年：2006
• 出版时间：26 June 2006
• 年：2006
• 卷：580
• 期：15
• 页码：3631-3637
• 全文大小：517 K

文摘

A trimeric protein phosphatase 2A (PP2A_T55) composed of the catalytic (PP2Ac), structural (PR65/A), and regulatory (PR55/B) subunits was isolated from rabbit skeletal muscle by thiophosphorylase affinity chromatography, and contained two additional proteins of 54 and 55 kDa, respectively. The 54 kDa protein was identified as eukaryotic translation termination factor 1 (eRF1) and as a PP2A interacting protein [Andjelkovic et al. (1996) EMBO J. 15, 101–112]. The 55 kDa protein is now identified as nucleoredoxin (NRX). The formation of a complex between GST–NRX, PP2A_C and PP2A_D was demonstrated by pull-down experiments with purified forms of PP2A, and by immunoprecipitation of HA-tagged NRX expressed in HEK293 cells complexed endogenous PP2A subunits. Analysis of PP2A activity in the presence of GST–NRX showed that NRX competed with polycations for both stimulatory and inhibitory effects on different forms of PP2A.