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Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function
Open accessAbstract
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 described, nor is it known whether the function of Pin1 is regulated. Here we show that Pin1 WW domain is phosphorylated on Ser(16) both in vitro and in vivo. Further, this phosphorylation regulates the ability of the WW domain to mediate Pin1 substrate interaction and cellular localization. Moreover, both Pin1 and WW domain mutants refractory to Ser(16) phosphorylation act as dominant-negative mutants to induce mitotic block and apoptosis and increase multinucleated cells with 8 N DNA content. Thus, phosphorylation is a new mechanism critical for regulating WW domain phosphoserine binding activity and Pin1 function.
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“It has been reported previously that phoshorylation of Ser16 of Pin1 impairs the function of Pin1 [12].”
From Prolyl Isomerase Pin1 Protects Mice from Endotoxin Shock (2011) · cites this paper as [12]
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Stout, J. M., Romero-Severson, E. O., Ruegger, M. O., & Chapple, C. C. S. (2008) · Genetics · doi:10.1534/genetics.107.083881 · Cited by 41
The role of Pin1 in the development and treatment of cancer
Min, S., Zhou, X. Z., & Lu, K. P. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0821-x · Cited by 41
Self-citationDeficiency of microRNA-628-5p promotes the progression of gastric cancer by upregulating PIN1
Chen, Y., Wu, Y., Yu, S., Yang, H., Wang, X., Zhang, Y., Zhu, S., Jie, M., Liu, C., Li, X., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02766-6 · Cited by 40
Prolyl isomerase Pin1 downregulates tumor suppressor RUNX3 in breast cancer
Tsang, Y.-H. N., Wu, X.-W., Lim, J.-S., Ong, C. W., Salto‐Tellez, M., Ito, K., Ito, Y., & Chen, L.-F. (2012) · Oncogene · doi:10.1038/onc.2012.178 · Cited by 40
Khanal, P., Kim, G., Lim, S., Yun, H., Lee, K. Y., Choi, H., & Choi, H. S. (2013) · The FASEB Journal · doi:10.1096/fj.13-236851 · Cited by 44
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Self-citationFan, G., Fan, Y., Gupta, N., Matsuura, I., Liu, F., Zhou, X. Z., Lu, K. P., & Gélinas, C. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4117 · Cited by 37
Self-citationRegulation of mitochondrial apoptosis by Pin1 in cancer and neurodegeneration
Sorrentino, G., Comel, A., Mantovani, F., & Sal, G. D. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.08.003 · Cited by 36
p66Shc in Cardiovascular Pathology
Haslem, L., Hays, J. M., & Hays, F. A. (2022) · Cells · doi:10.3390/cells11111855 · Cited by 37
Gonadotrophin‐Releasing Hormone Signalling Downstream of Calmodulin
Melamed, P., Savulescu, D. M., Lim, S. X., Wijeweera, A., Luo, Z., Luo, M., & Pnueli, L. (2012) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2012.02359.x · Cited by 39
Synthetic Receptors for the Differentiation of Phosphorylated Peptides with Nanomolar Affinities
Grauer, A., Riechers, A., Ritter, S., & König, B. (2008) · Chemistry - A European Journal · doi:10.1002/chem.200800432 · Cited by 36
Luo, Z., Wijeweera, A., Oh, Y., Liou, Y., & Melamed, P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00807-09 · Cited by 38
Self-citationNegative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1
Wang, X., Mahoney, B. J., Zhang, M., Zintsmaster, J. S., & Peng, J. W. (2015) · Structure · doi:10.1016/j.str.2015.08.019 · Cited by 35
Oncogenic Hijacking of the PIN1 Signaling Network
Zannini, A., Rustighi, A., Campaner, E., & Sal, G. D. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00094 · Cited by 37
Rudrabhatla, P., & Pant, H. C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1243 · Cited by 36
Metadata
- Authors
- Lu, P.-J., Zhou, X. Z., Liou, Y.-C., Noel, J. P., & Lu, K. P.
- Affiliations
- Beth Israel Deaconess Medical Center (US)
- Salk Institute for Biological Studies (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-01
- Volume
- 277
- Issue
- 4
- Pages
- 2381-2384
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1971696898
- Cited by
- 244
- References
- 28
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 15 · 2023: 6 · 2022: 6 · 2021: 2 · 2020: 11 · 2019: 4 · 2018: 7 · 2017: 2 · 2016: 10 · 2015: 17 · 2014: 13 · 2013: 16 · 2012: 21
- FWCI
- 3.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM 58556, R01GM058556, R01 GM 56230, R01GM056230)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- WW domain, Pin1, peptidyl-prolyl isomerase, Ser16 phosphorylation, substrate recognition, dominant-negative mutant, mitotic arrest, apoptosis, multinucleated cells, DNA ploidy, protein phosphorylation regulation
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Cell Cycle, DNA, Electrophoresis, Polyacrylamide Gel, Glutathione Transferase, HeLa Cells, Humans, Luminescent Proteins, Microscopy, Fluorescence, Mitosis, Mutation, Phosphorylation, Phosphoserine, Protein Binding, Recombinant Fusion Proteins, Serine, Threonine, Time Factors, Signal Transduction, Protein Structure, Tertiary, Peptidylprolyl Isomerase, Green Fluorescent Proteins
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