The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The PP1 binding code: a molecular‐lego strategy that governs specificity
Abstract
Ser/Thr protein phosphatase 1 (PP1) is a single‐domain hub protein with nearly 200 validated interactors in vertebrates. PP1‐interacting proteins (PIPs) are ubiquitously expressed but show an exceptional diversity in brain, testis and white blood cells. The binding of PIPs is mainly mediated by short motifs that dock to surface grooves of PP1. Although PIPs often contain variants of the same PP1 binding motifs, they differ in the number and combination of docking sites. This molecular‐lego strategy for binding to PP1 creates holoenzymes with unique properties. The PP1 binding code can be described as specific, universal, degenerate, nonexclusive and dynamic. PIPs control associated PP1 by interference with substrate recruitment or access to the active site. In addition, some PIPs have a subcellular targeting domain that promotes dephosphorylation by increasing the local concentration of PP1. The diversity of the PP1 interactome and the properties of the PP1 binding code account for the exquisite specificity of PP1 in vivo.
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Cites
A gene atlas of the mouse and human protein-encoding transcriptomes
Su, A. I., Wiltshire, T., Batalov, S., Lapp, H., Ching, K. A., Block, D., Zhang, J., Soden, R., Hayakawa, M., Kreiman, G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400782101 · Cited by 3,475
Structural mechanism of demethylation and inactivation of protein phosphatase 2A
Xing, Y., Li, Z., Chen, Y., Stock, J. B., Jeffrey, P. D., & Shi, Y. (2008) · Cell · doi:10.1016/j.cell.2008.02.041 · Cited by 206
Cited by
Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates
Brautigan, D. L., & Shenolikar, S. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012332 · Cited by 191
A PP1-PP2A phosphatase relay controls mitotic progression
Grallert, A., Boke, E., Hagting, A., Hodgson, B., Connolly, Y., Griffiths, J. R., Smith, D. L., Pines, J., & Hagan, I. M. (2015) · Nature · doi:10.1038/nature14019 · Cited by 188
PP2A-B′ holoenzyme substrate recognition, regulation and role in cytokinesis
Wu, C.-G., Chen, H., Guo, F., Yadav, V. K., Mcilwain, S. J., Rowse, M., Choudhary, A., Lin, Z., Li, Y., Gu, T., et al. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.27 · Cited by 85
PP1 and PP2A Use Opposite Phospho-dependencies to Control Distinct Processes at the Kinetochore
Smith, R. J., Cordeiro, M. H., Davey, N. E., Vallardi, G., Ciliberto, A., Gross, F., & Saurin, A. T. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.067 · Cited by 61
Metadata
- Authors
- Heroes, E., Lesage, B., Görnemann, J., Beullens, M., Van Meervelt, L., & Bollen, M.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2012-03-21
- Volume
- 280
- Issue
- 2
- Pages
- 584-595
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1484952182
- Cited by
- 316
- References
- 2
- FWCI
- 6.39
- 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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
