BIOMAT Database Logo BIOMAT Database Logo

Requirement of multiple protein domains and residues for gating K(ATP) channels by intracellular pH. 2001

H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Department of Biology, Georgia State University, Atlanta, Georgia 30302-4010, USA.

ATP-sensitive K(+) channels (K(ATP)) are regulated by pH in addition to ATP, ADP, and phospholipids. In the study we found evidence for the molecular basis of gating the cloned K(ATP) by intracellular protons. Systematic constructions of chimerical Kir6.2-Kir1.1 channels indicated that full pH sensitivity required the N terminus, C terminus, and M2 region. Three amino acid residues were identified in these protein domains, which are Thr-71 in the N terminus, Cys-166 in the M2 region, and His-175 in the C terminus. Mutation of any of them to their counterpart residues in Kir1.1 was sufficient to completely eliminate the pH sensitivity. Creation of these residues rendered the mutant channels clear pH-dependent activation. Thus, critical players in gating K(ATP) by protons are demonstrated. The pH sensitivity enables the K(ATP) to regulate cell excitability in a number of physiological and pathophysiological conditions when pH is low but ATP concentration is normal.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D009865 Oocytes Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM). Ovocytes,Oocyte,Ovocyte
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004594 Electrophysiology The study of the generation and behavior of electrical charges in living organisms particularly the nervous system and the effects of electricity on living organisms.
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000255 Adenosine Triphosphate An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. ATP,Adenosine Triphosphate, Calcium Salt,Adenosine Triphosphate, Chromium Salt,Adenosine Triphosphate, Magnesium Salt,Adenosine Triphosphate, Manganese Salt,Adenylpyrophosphate,CaATP,CrATP,Manganese Adenosine Triphosphate,MgATP,MnATP,ATP-MgCl2,Adenosine Triphosphate, Chromium Ammonium Salt,Adenosine Triphosphate, Magnesium Chloride,Atriphos,Chromium Adenosine Triphosphate,Cr(H2O)4 ATP,Magnesium Adenosine Triphosphate,Striadyne,ATP MgCl2
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Gating of inward-rectifier K+ channels by intracellular pH.
October 2000, European journal of biochemistry,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Gating of inward rectifier K(+) channels by proton-mediated interactions of intracellular protein domains.
January 2002, Trends in cardiovascular medicine,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
G proteins activate ATP-sensitive K+ channels by antagonizing ATP-dependent gating.
April 1994, Neuron,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
How RCK domains regulate gating of K+ channels.
September 2019, Biological chemistry,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Gating of two-pore domain K+ channels by extracellular pH.
November 2006, Biochemical Society transactions,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Gating and regulation of KCNH (ERG, EAG, and ELK) channels by intracellular domains.
December 2020, Channels (Austin, Tex.),
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Direct activation of cloned K(atp) channels by intracellular acidosis.
April 2001, The Journal of biological chemistry,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Effects of intracellular pH on ATP-sensitive K+ channels in mouse pancreatic beta-cells.
February 1994, The Journal of physiology,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Tandem function of nucleotide binding domains confers competence to sulfonylurea receptor in gating ATP-sensitive K+ channels.
April 2002, The Journal of biological chemistry,
H Piao, and N Cui, and H Xu, and J Mao, and A Rojas, and R Wang, and L Abdulkadir, and L Li, and J Wu, and C Jiang
Diadenosine tetraphosphate-gating of recombinant pancreatic ATP-sensitive K(+) channels.
February 2001, Bioscience reports,
Copied contents to your clipboard!