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

Science (New York, N.Y.) | Feb 26, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10037602

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.

Pubmed ID: 10037602 RIS Download

Mesh terms: Amino Acid Sequence | Amino Acid Substitution | Calcium-Binding Proteins | Cell Cycle Proteins | Endosomal Sorting Complexes Required for Transport | HeLa Cells | Humans | Ligases | Peptidylprolyl Isomerase | Phosphopeptides | Phosphoproteins | Phosphorylation | Phosphoserine | Phosphothreonine | Point Mutation | Signal Transduction | Ubiquitin-Protein Ligases | cdc25 Phosphatases

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Associated grants

  • Agency: NIGMS NIH HHS, Id: R01GM56230
  • Agency: NIGMS NIH HHS, Id: R01GM58556

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