ReviewFrontiers in pharmacology2015
Alterations in reversible protein histidine phosphorylation as intracellular signals in cardiovascular disease.
Review in Frontiers in pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- An Updated Review on Developing Small Molecule Kinase Inhibitors Using Computer-Aided Drug Design Approaches.International journal of molecular sciences · 2023Review
- Changes to Urinary Proteome in High-Fat-DietBiomolecules · 2022Article
- A global map of associations between types of protein posttranslational modifications and human genetic diseases.iScience · 2021Article
- Bis(zinc(II)-dipicolylamine)-functionalized sub-2 μm core-shell microspheres for the analysis of N-phosphoproteome.Nature communications · 2020Article
- NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020Review
- The Potential Functional Roles of NME1 Histidine Kinase Activity in Neuroblastoma Pathogenesis.International journal of molecular sciences · 2020Article
- Nucleoside Diphosphate Kinase B Contributes to Arrhythmogenesis in Human-Induced Pluripotent Stem Cell-Derived Cardiomyocytes from a Patient with Arrhythmogenic Right Ventricular Cardiomyopathy.Journal of clinical medicine · 2020Article
- Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation.The EMBO journal · 2019Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- Regulation of heterotrimeric G-protein signaling by NDPK/NME proteins and caveolins: an update.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- Histidine kinases and the missing phosphoproteome from prokaryotes to eukaryotes.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- Targeting altered Nme heterooligomerization in disease?Oncotarget · 2018Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reversible phosphorylation of amino acid side chains in proteins is a frequently used mechanism in cellular signal transduction and alterations of such phosphorylation patterns are very common in cardiovascular diseases. They reflect changes in the activities of the protein kinases and phosphatases involving signaling pathways. Phosphorylation of serine, threonine, and tyrosine residues has been extensively investigated in vertebrates, whereas reversible histidine phosphorylation, a well-known regulatory signal in lower organisms, has been largely neglected as it has been generally assumed that histidine phosphorylation is of minor importance in vertebrates. More recently, it has become evident that the nucleoside diphosphate kinase isoform B (NDPK-B), an ubiquitously expressed enzyme involved in nucleotide metabolism, and a highly specific phosphohistidine phosphatase (PHP) form a regulatory histidine protein kinase/phosphatase system in mammals. At least three well defined substrates of NDPK-B are known: The β-subunit of heterotrimeric G-proteins (Gβ), the intermediate conductance potassium channel SK4 and the Ca(2+) conducting TRP channel family member, TRPV5. In each of these proteins the phosphorylation of a specific histidine residue regulates cellular signal transduction or channel activity. This article will therefore summarize our current knowledge on protein histidine phosphorylation and highlight its relevance for cardiovascular physiology and pathophysiology.
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