Dimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilon.

ABSTRACT: cyt-PTP epsilon is a naturally occurring nonreceptor form of the receptor-type protein tyrosine phosphatase (PTP) epsilon. As such, cyt-PTP epsilon enables analysis of phosphatase regulation in the absence of extracellular domains, which participate in dimerization and inactivation of the receptor-type phosphatases receptor-type protein tyrosine phosphatase alpha (RPTPalpha) and CD45. Using immunoprecipitation and gel filtration, we show that cyt-PTP epsilon forms dimers and higher-order associations in vivo, the first such demonstration among nonreceptor phosphatases. Although cyt-PTP epsilon readily dimerizes in the absence of exogenous stabilization, dimerization is increased by oxidative stress. Epidermal growth factor receptor stimulation can affect cyt-PTP epsilon dimerization and ty

SUBMITTER: Toledano-Katchalski H 

PROVIDER: S-EPMC165729 | biostudies-literature | 2003 Aug

REPOSITORIES: biostudies-literature