Identification of proteins interacting with the catalytic subunit of PP2A by proteomics

Won Jeong Lee, Dong Uk Kim, Mi Young Lee, Kang Yell Choi

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The protein phosphatase 2A (PP2A) is a serine/threonine phosphatase involved in the regulation of multiple signaling pathways including the Wnt/β-catenin and the ERK pathways. To understand the complex signaling networking associated with PP2A, we searched proteins interacting with the catalytic subunit of protein phosphatase 2A (PP2Ac) by a pull-down analysis followed by 2-D gel electrophoresis and proteomic analyses. The probability of identification of the proteins interacting with PP2Ac was increased by searching proteins differently interacting with PP2Ac according to stimulation of Wnt3a, which regulates both the Wnt/β-catenin and the ERK pathways. Around 100 proteins, pulled-down by His-tagged PP2Ac, were identified in 2-D gels stained with CBB. By MALDI-TOF-MS analyses of 45 protein spots, we identified several proteins that were previously known to interact with PP2A, such as Axin and CaMK IV. In addition, we also identified many proteins that potentially interact with PP2Ac. The interactions of several candidate proteins, such as tuberous sclerosis complex 2, RhoB, R-Ras, and Nm23H2, with PP2Ac, were confirmed by in vitro binding analyses and/or coimmunoprecipitation experiments.

Original languageEnglish
Pages (from-to)206-214
Number of pages9
JournalProteomics
Volume7
Issue number2
DOIs
Publication statusPublished - 2007 Jan

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Identification of proteins interacting with the catalytic subunit of PP2A by proteomics'. Together they form a unique fingerprint.

  • Cite this