The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
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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Self-citation
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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