Bioinformatic Analysis of Na+, K+-ATPase Regulation through Phosphorylation of the Alpha-Subunit N-Terminus.
- Publisher:
- MDPI
- Publication Type:
- Journal Article
- Citation:
- Int J Mol Sci, 2023, 24, (1), pp. 67
- Issue Date:
- 2023
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Blayney, E-L | |
dc.contributor.author | Chennath, M | |
dc.contributor.author | Cranfield, CG | |
dc.contributor.author | Clarke, RJ | |
dc.date.accessioned | 2024-01-16T00:32:23Z | |
dc.date.available | 2022-12-17 | |
dc.date.available | 2024-01-16T00:32:23Z | |
dc.date.issued | 2023 | |
dc.identifier.citation | Int J Mol Sci, 2023, 24, (1), pp. 67 | |
dc.identifier.issn | 1422-0067 | |
dc.identifier.issn | 1422-0067 | |
dc.identifier.uri | http://hdl.handle.net/10453/174517 | |
dc.description.abstract | The Na+, K+-ATPase is an integral membrane protein which uses the energy of ATP hydrolysis to pump Na+ and K+ ions across the plasma membrane of all animal cells. It plays crucial roles in numerous physiological processes, such as cell volume regulation, nutrient reabsorption in the kidneys, nerve impulse transmission, and muscle contraction. Recent data suggest that it is regulated via an electrostatic switch mechanism involving the interaction of its lysine-rich N-terminus with the cytoplasmic surface of its surrounding lipid membrane, which can be modulated through the regulatory phosphorylation of the conserved serine and tyrosine residues on the protein's N-terminal tail. Prior data indicate that the kinases responsible for phosphorylation belong to the protein kinase C (PKC) and Src kinase families. To provide indications of which particular enzyme of these families might be responsible, we analysed them for evidence of coevolution via the mirror tree method, utilising coevolution as a marker for a functional interaction. The results obtained showed that the most likely kinase isoforms to interact with the Na+, K+-ATPase were the θ and η isoforms of PKC and the Src kinase itself. These theoretical results will guide the direction of future experimental studies. | |
dc.format | Electronic | |
dc.language | eng | |
dc.publisher | MDPI | |
dc.relation.ispartof | Int J Mol Sci | |
dc.relation.isbasedon | 10.3390/ijms24010067 | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | 0399 Other Chemical Sciences, 0604 Genetics, 0699 Other Biological Sciences | |
dc.subject.classification | Chemical Physics | |
dc.subject.classification | 3101 Biochemistry and cell biology | |
dc.subject.classification | 3107 Microbiology | |
dc.subject.classification | 3404 Medicinal and biomolecular chemistry | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Ions | |
dc.subject.mesh | Phosphorylation | |
dc.subject.mesh | Protein Kinase C | |
dc.subject.mesh | Sodium-Potassium-Exchanging ATPase | |
dc.subject.mesh | src-Family Kinases | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Phosphorylation | |
dc.subject.mesh | Sodium-Potassium-Exchanging ATPase | |
dc.subject.mesh | src-Family Kinases | |
dc.subject.mesh | Protein Kinase C | |
dc.subject.mesh | Ions | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Ions | |
dc.subject.mesh | Protein Kinase C | |
dc.subject.mesh | src-Family Kinases | |
dc.subject.mesh | Phosphorylation | |
dc.subject.mesh | Sodium-Potassium-Exchanging ATPase | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Phosphorylation | |
dc.subject.mesh | Sodium-Potassium-Exchanging ATPase | |
dc.subject.mesh | src-Family Kinases | |
dc.subject.mesh | Protein Kinase C | |
dc.subject.mesh | Ions | |
dc.title | Bioinformatic Analysis of Na+, K+-ATPase Regulation through Phosphorylation of the Alpha-Subunit N-Terminus. | |
dc.type | Journal Article | |
utslib.citation.volume | 24 | |
utslib.location.activity | Switzerland | |
utslib.for | 0399 Other Chemical Sciences | |
utslib.for | 0604 Genetics | |
utslib.for | 0699 Other Biological Sciences | |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
pubs.organisational-group | /University of Technology Sydney/Centre for Health Technologies (CHT) | |
utslib.copyright.status | open_access | * |
pubs.consider-herdc | false | |
dc.date.updated | 2024-01-16T00:32:18Z | |
pubs.issue | 1 | |
pubs.publication-status | Published online | |
pubs.volume | 24 | |
utslib.citation.issue | 1 |
Abstract:
The Na+, K+-ATPase is an integral membrane protein which uses the energy of ATP hydrolysis to pump Na+ and K+ ions across the plasma membrane of all animal cells. It plays crucial roles in numerous physiological processes, such as cell volume regulation, nutrient reabsorption in the kidneys, nerve impulse transmission, and muscle contraction. Recent data suggest that it is regulated via an electrostatic switch mechanism involving the interaction of its lysine-rich N-terminus with the cytoplasmic surface of its surrounding lipid membrane, which can be modulated through the regulatory phosphorylation of the conserved serine and tyrosine residues on the protein's N-terminal tail. Prior data indicate that the kinases responsible for phosphorylation belong to the protein kinase C (PKC) and Src kinase families. To provide indications of which particular enzyme of these families might be responsible, we analysed them for evidence of coevolution via the mirror tree method, utilising coevolution as a marker for a functional interaction. The results obtained showed that the most likely kinase isoforms to interact with the Na+, K+-ATPase were the θ and η isoforms of PKC and the Src kinase itself. These theoretical results will guide the direction of future experimental studies.
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