ArticleFrontiers in physiology2013
Non-catalytic participation of the Pin1 peptidyl-prolyl isomerase domain in target binding.
Article in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Phosphorylation in the dynein light intermediate chain 2 isoform enables Pin1 binding and modulates cargo-adaptor interactions.Journal of structural biology: X · 2026Article
- A tethering mechanism underlies Pin1-catalyzed prolineProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent.Biochemistry · 2024Article
- Dissecting the functional behavior of the differentially phosphorylated prolyl isomerase, Pin1.Protein science : a publication of the Protein Society · 2024Article
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- The Peptidyl-ProlylFrontiers in immunology · 2023Article
- Regulation of eukaryotic protein kinases by Pin1, a peptidyl-prolyl isomerase.Advances in biological regulation · 2023Article
- Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.Communications biology · 2021Article
- Activity-dependent isomerization of Kv4.2 by Pin1 regulates cognitive flexibility.Nature communications · 2020Article
- Activity and Affinity of Pin1 Variants.Molecules (Basel, Switzerland) · 2019Review
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- Structural and cellular mechanisms of peptidyl-prolyl isomerase Pin1-mediated enhancement of Tissue Factor gene expression, protein half-life, and pro-coagulant activity.Haematologica · 2018Article
- Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1.Frontiers in oncology · 2018Review
- PIN1 in breast development and cancer: a clinical perspective.Cell death and differentiation · 2017Review
- Neighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding.The FEBS journal · 2016Article
- G Protein-coupled Receptor Kinase 2 (GRK2) Promotes Breast Tumorigenesis Through a HDAC6-Pin1 Axis.EBioMedicine · 2016Article
- Cell cycle-dependent phosphorylation of nucleophosmin and its potential regulation by peptidyl-prolyl cis/trans isomerase.Journal of molecular biochemistry · 2015Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- Investigating Dynamic Interdomain Allostery in Pin1.Biophysical reviews · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pin1 is a phosphorylation-dependent peptidyl-prolyl isomerase (PPIase) that has the potential to add an additional level of regulation within protein kinase mediated signaling pathways. Furthermore, there is a mounting body of evidence implicating Pin1 in the emergence of pathological phenotypes in neurodegeneration and cancer through the isomerization of a wide variety of substrates at peptidyl-prolyl bonds where the residue preceding proline is a phosphorylated serine or threonine residue (i.e., pS/T-P motifs). A key step in this regulatory process is the interaction of Pin-1 with its substrates. This is a complex process since Pin1 is composed of two domains, the catalytic PPIase domain, and a type IV WW domain, both of which recognize pS/T-P motifs. The observation that the WW domain exhibits considerably higher binding affinity for pS/T-P motifs has led to predictions that the two domains may have distinct roles in mediating the actions of Pin1 on its substrates. To evaluate the participation of its individual domains in target binding, we performed GST pulldowns to monitor interactions between various forms of Pin1 and mitotic phospho-proteins that revealed two classes of Pin-1 interacting proteins, differing in their requirement for residues within the PPIase domain. From these observations, we consider models for Pin1-substrate interactions and the potential functions of the different classes of Pin1 interacting proteins. We also compare sequences that are recognized by Pin1 within its individual interaction partners to investigate the underlying basis for its different types of interactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.