Function of WW domains as phosphoserine- or phosphothreonine-binding modules

Pei Jung Lu, Xiao Zhen Zhou, Minhui Shen, Kun Ping Lu

Research output: Contribution to journalArticlepeer-review

552 Citations (Scopus)

Abstract

Protein-interacting modules help determine the specificity of signal transduction events, and protein phosphorylation can modulate the assembly of such modules into specific signaling complexes. Although phosphotyrosine- binding modules have been well-characterized, phosphoserine- or phosphothreonine-binding modules have not been described. WW domains are small protein modules found in various proteins that participate in cell signaling or regulation. WW domains of the essential mitotic prolyl isomerase Pin1 and the ubiquitin ligase Nedd4 bound to phosphoproteins, including physiological substrates of enzymes, in a phosphorylation-dependent manner. The Pin1 WW domain functioned as a phosphoserine- or phosphothreonine- binding module, with properties similar to those of SRC homology 2 domains. Phosphoserine- or phosphothreonine-binding activity was required for Pin1 to interact with its substrates in vitro and to perform its essential function in vivo.

Original languageEnglish
Pages (from-to)1325-1328
Number of pages4
JournalScience
Volume283
Issue number5406
DOIs
Publication statusPublished - 1999 Feb 26

All Science Journal Classification (ASJC) codes

  • General

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