ArticleThe Journal of cell biology2013
Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.
Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Proline-directed phosphorylation and prolyl isomerization oppose each other to regulate PSD-95 ubiquitination and excitatory synaptic plasticity.Frontiers in molecular neuroscience · 2026Article
- Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021Review
- Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain.Nucleic acids research · 2020Article
- FKBP25 participates in DNA double-strand break repair.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2020Article
- Linker histone H1.5 is an underestimated factor in differentiation and carcinogenesis.Environmental epigenetics · 2020Review
- Pinning Down the Transcription: A Role for Peptidyl-ProlylFrontiers in cell and developmental biology · 2020Review
- Molecular Mechanism of the Pin1-Histone H1 Interaction.Biochemistry · 2019Article
- Oncogenic Hijacking of the PIN1 Signaling Network.Frontiers in oncology · 2019Review
- A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study.Journal of biomolecular NMR · 2018Article
- Identification of a novel cAMP dependent protein kinase A phosphorylation site on the human cardiac calcium channel.Scientific reports · 2017Article
- Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Chromosoma · 2017Review
- Linker Histone in Diseases.International journal of biological sciences · 2017Review
- A brief review of nucleosome structure.FEBS letters · 2015Review
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- KSHV reactivation and novel implications of protein isomerization on lytic switch control.Viruses · 2015Review
- Review
- NF-κB transcriptional activity is modulated by FK506-binding proteins FKBP51 and FKBP52: a role for peptidyl-prolyl isomerase activity.The Journal of biological chemistry · 2014Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Histone H1 plays a crucial role in stabilizing higher order chromatin structure. Transcriptional activation, DNA replication, and chromosome condensation all require changes in chromatin structure and are correlated with the phosphorylation of histone H1. In this study, we describe a novel interaction between Pin1, a phosphorylation-specific prolyl isomerase, and phosphorylated histone H1. A sub-stoichiometric amount of Pin1 stimulated the dephosphorylation of H1 in vitro and modulated the structure of the C-terminal domain of H1 in a phosphorylation-dependent manner. Depletion of Pin1 destabilized H1 binding to chromatin only when Pin1 binding sites on H1 were present. Pin1 recruitment and localized histone H1 phosphorylation were associated with transcriptional activation independent of RNA polymerase II. We thus identify a novel form of histone H1 regulation through phosphorylation-dependent proline isomerization, which has consequences on overall H1 phosphorylation levels and the stability of H1 binding to chromatin.
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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.