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Article

Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function.

The Journal of biological chemistry - 25 Jan 2002

Lu Pei-Jung, Zhou Xiao Zhen, Liou Yih-Cherng, Noel Joseph P, Lu Kun Ping

Abstract excerpt

Phosphoserine-binding modules help determine the specificity of signal transduction events. One such module, the group IV WW domain, plays an essential role in targeting the phosphorylation-specific prolyl isomerase Pin1 to its substrates. These modules require Ser/Thr phosphorylation of their ligands for binding activity. However, phosphorylation of these modules and its functional significance have not been...

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Identifiers

PMID: 11723108
DOI: 10.1074/jbc.C100228200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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