The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding Modules
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.
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Cites
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
How Proteolysis Drives the Cell Cycle
King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273
Modular binding domains in signal transduction proteins
Cohen, G. B., Ren, R., & Baltimore, D. (1995) · Cell · doi:10.1016/0092-8674(95)90406-9 · Cited by 951
Radhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., & Wright, P. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80463-8 · Cited by 728
Structure and function of the WW domain
Sudol, M. (1996) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(96)00008-9 · Cited by 296
Cited by
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
Yeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1110 · Cited by 791
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721
Self-citationThe prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682
Self-citationThe prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production
Pastorino, L., Sun, A., Lu, P.-J., Zhou, X. Z., Balastik, M., Finn, G., Wulf, G., Lim, J., Li, S.-H., Li, X., et al. (2006) · Nature · doi:10.1038/nature04543 · Cited by 487
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Metadata
- Authors
- Lu, P.-J., Zhou, X. Z., Shen, M., & Lu, K. P.
- Venue
- Science
- Published
- 1999-02-26
- Volume
- 283
- Issue
- 5406
- Pages
- 1325-1328
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2050779639
- Cited by
- 682
- References
- 5
- FWCI
- 16.86
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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