ReviewJournal of bioenergetics and biomembranes2007
Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2-ATPase, the gatekeeper and the pivot.
Review in Journal of bioenergetics and biomembranes, 2007. 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, 20 citations in OpenAlex.
- An Intracellular Pathway Controlled by the N-terminus of the Pump Subunit Inhibits the Bacterial KdpFABC Ion Pump in High KJournal of molecular biology · 2021Article
- Structure of the human plasma membrane CaNature communications · 2018Article
- Improved Model of Proton Pump Crystal Structure Obtained by Interactive Molecular Dynamics Flexible Fitting Expands the Mechanistic Model for Proton Translocation in P-Type ATPases.Frontiers in physiology · 2017Article
- Sequential substitution of K(+) bound to Na(+),K(+)-ATPase visualized by X-ray crystallography.Nature communications · 2015Article
- Somatic mutations of the ATP1A1 gene and aldosterone-producing adenomas.Molecular and cellular endocrinology · 2015Review
- Hyperactivation of the human plasma membrane Ca2+ pump PMCA h4xb by mutation of Glu99 to Lys.The Journal of biological chemistry · 2014Article
- Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase.The Journal of biological chemistry · 2013Review
- A conserved asparagine in a P-type proton pump is required for efficient gating of protons.The Journal of biological chemistry · 2013Article
- Article
- Na(+),K (+)-ATPase as a docking station: protein-protein complexes of the Na(+),K (+)-ATPase.Cellular and molecular life sciences : CMLS · 2013Review
- Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease.Journal of bioenergetics and biomembranes · 2007Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this review we summarize mutagenesis work on the structure-function relationship of transmembrane segment M1 in the Na+,K+-ATPase and the sarco(endo)plasmic reticulum Ca2+-ATPase. The original hypothesis that charged residues in the N-terminal part of M1 interact with the transported cations can be rejected. On the other hand hydrophobic residues in the middle part of M1 turned out to play crucial roles in Ca2+ interaction/occlusion in Ca2+-ATPase and K+ interaction/occlusion in Na+,K+-ATPase. Leu65 of the Ca2+-ATPase and Leu99 of the Na+,K+-ATPase, located at homologous positions in M1, function as gate-locking residues that restrict the mobility of the side chain of the cation binding/gating residue of transmembrane segment M4, Glu309/Glu329. A pivot formed between a pair of a glycine and a bulky residue in M1 and M3 seems critical to the opening of the extracytoplasmic gate in both the Ca2+-ATPase and the Na+,K+-ATPase.
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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.