Membrane Topology of the α Subunit of Na,K-ATPase

1994 ◽  
pp. 358-361 ◽  
Author(s):  
M. Mohraz ◽  
E. Arystarkhova ◽  
K. J. Sweadner
Keyword(s):  
Membrane Topology ◽  
Α Subunit

Corrigendum to: In silico characterisation and functional validation of chilling tolerant divergence 1 (COLD1) gene in monocots during abiotic stress

2019 ◽  
Vol 46 (6) ◽  
pp. 596
Author(s):  
P. Anunanthini ◽  
V. M. Manoj ◽  
T. S. Sarath Padmanabhan ◽  
S. Dhivya ◽  
J. Ashwin Narayan ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
G Protein ◽  
Oryza Sativa L ◽  
Membrane Topology ◽  
G Protein Coupled Receptor ◽  
Crop Species ◽  
Α Subunit ◽  
Expression Studies ◽  
Gene Expression Studies ◽  
G Protein Coupled

The G protein-coupled receptor is one of the major transmembrane proteins in plants. It consists of an α subunit, a β subunit and three γ subunits. Chilling tolerant divergence 1 (COLD1) includes a Golgi pH receptor (GPHR) domain, which maintains cell membrane organisation and dynamics, along with abscisic acid linked G protein-coupled receptor (ABA_GPCR) that regulates the signalling pathways during cold stress. In the present study, we performed characterisation of a homologous COLD1 from the economically important monocot species Oryza sativa L., Zea mays L., Sorghum bicolor (L.)Moench and Erianthus arundinaceus (L.) Beauv. IK 76-81, a wild relative of Saccharum. COLD1 was isolated from E. arundinaceus IK 76-81, analysed for its evolution, domain, membrane topology, followed by prediction of secondary, tertiary structures and functionally validated in all four different monocots. Gene expression studies of COLD1 revealed differential expression under heat, drought, salinity and cold stresses in selected monocots. This is the first study on regulation of native COLD1 during abiotic stress in monocots, which has opened up new leads for trait improvement strategies in this economically important crop species.

In silico characterisation and functional validation of chilling tolerant divergence 1 (COLD1) gene in monocots during abiotic stress

2019 ◽  
Vol 46 (6) ◽  
pp. 524 ◽  
Author(s):  
P. Anunanthini ◽  
V. M. Manoj ◽  
T. S. Sarath Padmanabhan ◽  
S. Dhivya ◽  
J. Ashwin Narayan ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
G Protein ◽  
Oryza Sativa L ◽  
Membrane Topology ◽  
G Protein Coupled Receptor ◽  
Crop Species ◽  
Α Subunit ◽  
Expression Studies ◽  
Gene Expression Studies ◽  
G Protein Coupled

The G protein-coupled receptor is one of the major transmembrane proteins in plants. It consists of an α subunit, a β subunit and three γ subunits. Chilling tolerant divergence 1 (COLD1) includes a Golgi pH receptor (GPHR) domain, which maintains cell membrane organisation and dynamics, along with abscisic acid linked G protein-coupled receptor (ABA_GPCR) that regulates the signalling pathways during cold stress. In the present study, we performed characterisation of a homologous COLD1 from the economically important monocot species Oryza sativa L., Zea mays L., Sorghum bicolor (L.)Moench and Erianthus arundinaceus (L.) Beauv. IK 76-81, a wild relative of Saccharum. COLD1 was isolated from E. arundinaceus IK 76-81, analysed for its evolution, domain, membrane topology, followed by prediction of secondary, tertiary structures and functionally validated in all four different monocots. Gene expression studies of COLD1 revealed differential expression under heat, drought, salinity and cold stresses in selected monocots. This is the first study on regulation of native COLD1 during abiotic stress in monocots, which has opened up new leads for trait improvement strategies in this economically important crop species.

cDNA cloning and membrane topology of the rabbit gastric H+/K+-ATPase α-subunit

1992 ◽  
Vol 1131 (1) ◽  
pp. 69-77 ◽  
Author(s):  
Krister Bamberg ◽  
Frederic Mercier ◽  
Michael A. Reuben ◽  
Yutaka Kobayashi ◽  
Keith B. Munson ◽  
...  
Keyword(s):  
Cdna Cloning ◽  
Membrane Topology ◽  
Α Subunit

scholarly journals H,K-ATPase α subunit C-terminal membrane topology: epitope tags in the insect cell expression system

1999 ◽  
Vol 340 (3) ◽  
pp. 601 ◽  
Author(s):  
Adam J. SMOLKA ◽  
Kellie A. LARSEN ◽  
Clifford W. SCHWEINFEST ◽  
Charles E. HAMMOND
Keyword(s):  
Insect Cell ◽  
Expression System ◽  
Membrane Topology ◽  
Α Subunit ◽  
Subunit C ◽  
Insect Cell Expression System ◽  
Cell Expression ◽  
Insect Cell Expression ◽  
Cell Expression System

A role for mammalian Ubc6 homologues in ER-associated protein degradation

2002 ◽  
Vol 115 (14) ◽  
pp. 3007-3014 ◽  
Author(s):  
Uwe Lenk ◽  
Helen Yu ◽  
Jan Walter ◽  
Marina S. Gelman ◽  
Enno Hartmann ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Receptor ◽  
Dominant Negative ◽  
Membrane Topology ◽  
Secretory Proteins ◽  
Mutant Form ◽  
Α Subunit ◽  
Ubiquitin Conjugating Enzyme ◽  
Biochemical Analyses ◽  
Related Proteins

Integral membrane and secretory proteins which fail to fold productively are retained in the endoplasmic reticulum and targeted for degradation by cytoplasmic proteasomes. Genetic and biochemical analyses suggest that substrates of this pathway must be dislocated across the membrane of the endoplasmic reticulum (ER) by a process requiring a functional Sec61 complex and multiubiquitinylation. In yeast, the tail-anchored ubiquitin-conjugating enzyme Ubc6p, which is localized to the cytoplasmic surface of the ER,participates in ER-associated degradation (ERAD) of misfolded proteins. Here we describe the identification of two families of mammalian Ubc6p-related proteins. Members of both families are also located in the ER membrane and display a similar membrane topology as the yeast enzyme. Furthermore we show that expression of elevated levels of wild-type and dominant-negative alleles of these components affects specifically ERAD of the α subunit of the T-cell receptor and a mutant form of the CFTR protein. Similarly, we describe that the expression level of Ubc6p in yeast is also critical for ERAD,suggesting that the Ubc6p function is highly conserved from yeast to mammals.

V. The epithelial sodium channel and its implication in human diseases

1999 ◽  
Vol 276 (3) ◽  
pp. G567-G571 ◽  
Author(s):  
Edith Hummler ◽  
Jean-Daniel Horisberger
Keyword(s):  
Distal Colon ◽  
Loss Of Function ◽  
Newborn Mice ◽  
Α Subunit ◽  
Salt Wasting ◽  
Lung Fluid ◽  
Wasting Syndrome ◽  
Rate Limiting Step ◽  
Γ Subunit ◽  
Rate Limiting

The epithelial Na+ channel (ENaC) controls the rate-limiting step in the process of transepithelial Na+ reabsorption in the distal nephron, the distal colon, and the airways. Hereditary salt-losing syndromes have been ascribed to loss of function mutations in the α-, β-, or γ-ENaC subunit genes, whereas gain of function mutations (located in the COOH terminus of the β- or γ-subunit) result in hypertension due to Na+ retention (Liddle’s syndrome). In mice, gene-targeting experiments have shown that, in addition to the kidney salt-wasting phenotype, ENaC was essential for lung fluid clearance in newborn mice. Disruption of the α-subunit resulted in a complete abolition of ENaC-mediated Na+ transport, whereas knockout of the β- or γ-subunit had only minor effects on fluid clearance in lung. Disruption of each of the three subunits resulted in a salt-wasting syndrome similar to that observed in humans.

scholarly journals Maturation of the Na,K-ATPase in the Endoplasmic Reticulum in Health and Disease

2021 ◽  
Author(s):  
Vitalii Kryvenko ◽  
Olga Vagin ◽  
Laura A. Dada ◽  
Jacob I. Sznajder ◽  
István Vadász
Keyword(s):  
Endoplasmic Reticulum ◽  
Intracellular Signaling ◽  
Loss Of Function ◽  
Α Subunit ◽  
Rate Limiting Step ◽  
Atpase Subunits ◽  
A Cell ◽  
Health And Disease ◽  
And Function ◽  
Rate Limiting

Abstract The Na,K-ATPase establishes the electrochemical gradient of cells by driving an active exchange of Na+ and K+ ions while consuming ATP. The minimal functional transporter consists of a catalytic α-subunit and a β-subunit with chaperon activity. The Na,K-ATPase also functions as a cell adhesion molecule and participates in various intracellular signaling pathways. The maturation and trafficking of the Na,K-ATPase include co- and post-translational processing of the enzyme in the endoplasmic reticulum (ER) and the Golgi apparatus and subsequent delivery to the plasma membrane (PM). The ER folding of the enzyme is considered as the rate-limiting step in the membrane delivery of the protein. It has been demonstrated that only assembled Na,K-ATPase α:β-complexes may exit the organelle, whereas unassembled, misfolded or unfolded subunits are retained in the ER and are subsequently degraded. Loss of function of the Na,K-ATPase has been associated with lung, heart, kidney and neurological disorders. Recently, it has been shown that ER dysfunction, in particular, alterations in the homeostasis of the organelle, as well as impaired ER-resident chaperone activity may impede folding of Na,K-ATPase subunits, thus decreasing the abundance and function of the enzyme at the PM. Here, we summarize our current understanding on maturation and subsequent processing of the Na,K-ATPase in the ER under physiological and pathophysiological conditions. Graphic Abstract

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