Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains

MJ Wishart, JE Dixon - Trends in biochemical sciences, 1998 - cell.com
MJ Wishart, JE Dixon
Trends in biochemical sciences, 1998cell.com
The effects of tyrosine phosphorylation are manifested and regulated through protein
domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain
found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo.
Individual STYX domains are not catalytically active; however, they resemble protein
tyrosine phosphatase (PTP) domains and, like PTPs, contain core sequences that recognize
phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular …
Abstract
The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not catalytically active; however, they resemble protein tyrosine phosphatase (PTP) domains and, like PTPs, contain core sequences that recognize phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation.
cell.com