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

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

研究成果: Article同行評審

587 引文 斯高帕斯(Scopus)


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.

頁(從 - 到)1325-1328
出版狀態Published - 1999 2月 26

All Science Journal Classification (ASJC) codes

  • 多學科


深入研究「Function of WW domains as phosphoserine- or phosphothreonine-binding modules」主題。共同形成了獨特的指紋。