ArticleBiochemistry2019
Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Cellular Consequences, Citrullination Substrates, and Antigenicity of Targeting PAD4 to Cell Surfaces.ACS central science · 2026Article
- Unveiling nuclear localization signals in human arginine deiminase proteins.Protein science : a publication of the Protein Society · 2026Article
- Cellular consequences, citrullination substrates, and antigenicity resulting from wild-type and targeted PAD4 on cell surfaces.bioRxiv : the preprint server for biology · 2026Article
- Bibliometric and visualization analysis of arginine deiminase research from 2006 to 2025: trends, collaboration networks and emerging frontiers.Frontiers in immunology · 2026Article
- Peptidylarginine Deiminases: An Overview of Recent Advances in Citrullination Research.International journal of molecular sciences · 2025Review
- Citrullination in Tumor Metastasis, Inside and Outside the Cells.Cancer science · 2025Review
- Sex-dependent effects of peptidylarginine deiminases on neutrophil function and long-term outcomes after spinal cord injury.Experimental neurology · 2025Article
- A citrullinated histone H3 monoclonal antibody for immune modulation in sepsis.Nature communications · 2025Article
- Citrullination in health and disease: From physiological function to gene regulation.Genes & diseases · 2025Review
- Citrullination and the protein code: crosstalk between post-translational modifications in cancer.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Review
- Fusobacterium nucleatum-triggered neutrophil extracellular traps facilitate colorectal carcinoma progression.Journal of experimental & clinical cancer research : CR · 2023Article
- PADs and NETs in digestive system: From physiology to pathology.Frontiers in immunology · 2023Review
- Peptidylarginine deiminase enzymes and citrullinated proteins in female reproductive physiology and associated diseases†.Biology of reproduction · 2022Review
- PAD4 and Its Inhibitors in Cancer Progression and Prognosis.Pharmaceutics · 2022Review
- The virtues and vices of protein citrullination.Royal Society open science · 2022Review
- The Citrullination-Neutrophil Extracellular Trap Axis in Chronic Diseases.Journal of innate immunity · 2022Review
- Proximity-Dependent Labeling of Cysteines.Journal of the American Chemical Society · 2021Article
- A Streamlined Data Analysis Pipeline for the Identification of Sites of Citrullination.Biochemistry · 2021Article
- Progesterone stimulates histone citrullination to increase IGFBP1 expression in uterine cells.Reproduction (Cambridge, England) · 2021Article
- Applicability of Small-Molecule Inhibitors in the Study of Peptidyl Arginine Deiminase 2 (PAD2) and PAD4.Frontiers in immunology · 2021Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Protein arginine deiminases (PADs) are calcium-dependent enzymes that mediate the post-translational conversion of arginine into citrulline. Dysregulated PAD activity is associated with numerous autoimmune disorders and cancers. In breast cancer, PAD2 citrullinates histone H3R26 and activates the transcription of estrogen receptor target genes. However, PAD2 lacks a canonical nuclear localization sequence, and it is unclear how this enzyme is transported into the nucleus. Here, we show for the first time that PAD2 translocates into the nucleus in response to calcium signaling. Using BioID2, a proximity-dependent biotinylation method for identifying interacting proteins, we found that PAD2 preferentially associates with ANXA5 in the cytoplasm. Binding of calcium to PAD2 weakens this cytoplasmic interaction, which generates a pool of calcium-bound PAD2 that can interact with Ran. We hypothesize that this latter interaction promotes the translocation of PAD2 into the nucleus. These findings highlight a critical role for ANXA5 in regulating PAD2 and identify an unusual mechanism whereby proteins translocate between the cytosol and nucleus.
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Registered trials
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.