Transcriptional regulation by glucose of the yeastPMA1 gene encoding the plasma membrane H+-ATPase

Yeast ◽  
1993 ◽  
Vol 9 (10) ◽  
pp. 1075-1084 ◽  
Author(s):  
Rajini Rao ◽  
Daniela Drummond-Barbosa ◽  
Carolyn W. Slayman
Keyword(s):  
Transcriptional Regulation ◽  
Plasma Membrane ◽  
Gene Encoding

Opposing effects of podocin on the gating of podocyte TRPC6 channels evoked by membrane stretch or diacylglycerol

2013 ◽  
Vol 305 (3) ◽  
pp. C276-C289 ◽  
Author(s):  
Marc Anderson ◽  
Eun Young Kim ◽  
Henning Hagmann ◽  
Thomas Benzing ◽  
Stuart E. Dryer
Keyword(s):  
Plasma Membrane ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Stretch Activation ◽  
Gain Of Function ◽  
Gene Encoding ◽  
Membrane Stretch ◽  
Transient Receptor ◽  
Opposing Effects ◽  
Interfering Rna

Gain-of-function mutations in the transient receptor potential (TRP) cation channel subfamily C member 6 ( TRPC6) gene and mutations in the NPHS2 gene encoding podocin result in nephrotic syndromes. The purpose of this study was to determine the functional significance of biochemical interactions between these proteins. We observed that gating of TRPC6 channels in podocytes is markedly mechanosensitive and can be activated by hyposmotic stretch or indentation of the plasma membrane. Stretch activation of cationic currents was blocked by small interfering RNA knockdown of TRPC6, as well as by SKF-96365 or micromolar La3+. Stretch activation of podocyte TRPC6 persisted in the presence of inhibitors of phospholipase C (U-73122) and phospholipase A2 (ONO-RS-082). Robust stretch responses also persisted when recording electrodes contained guanosine 5′- O-(2-thiodiphosphate) at concentrations that completely suppressed responses to ANG II. Stretch responses were enhanced by cytochalasin D but were abolished by the peptide GsMTx4, suggesting that forces are transmitted to the channels through the plasma membrane. Podocin and TRPC6 interact at their respective COOH termini. Knockdown of podocin markedly increased stretch-evoked activation of TRPC6 but nearly abolished TRPC6 activation evoked by a diacylglycerol analog. These data suggest that podocin acts as a switch to determine the preferred mode of TRPC6 activation. They also suggest that podocin deficiencies will result in Ca2+ overload in foot processes, as with gain-of-function mutations in the TRPC6 gene. Finally, they suggest that mechanical activation of TRP family channels and the preferred mode of TRP channel activation may depend on whether members of the stomatin/prohibitin family of hairpin loop proteins are present.

scholarly journals Autogenous Transcriptional Regulation of the regA Gene, Encoding an AraC-Like, Essential Virulence Regulator in Citrobacter rodentium

2011 ◽  
Vol 193 (7) ◽  
pp. 1777-1782 ◽  
Author(s):  
A. Tan ◽  
J. Yang ◽  
M. Tauschek ◽  
J. Praszkier ◽  
R. M. Robins-Browne
Keyword(s):  
Transcriptional Regulation ◽  
Citrobacter Rodentium ◽  
Gene Encoding ◽  
Virulence Regulator

scholarly journals Progress Toward The Synthesis Of Labeled Derivatives Of The Cystic Fibrosis Drug Ivacaftor

2021 ◽  
Author(s):  
Salma Elmallah
Keyword(s):  
Cystic Fibrosis ◽  
Plasma Membrane ◽  
Genetic Diseases ◽  
Early Death ◽  
Open Probability ◽  
Gene Encoding ◽  
Short Period ◽  
Cftr Mutations ◽  
Cftr Protein ◽  
Orally Bioavailable

Cystic fibrosis (CF) is one of the most common genetic diseases, affecting approximately 70,000 people worldwide causing severe complications and often leading to early death. CF is caused by a mutation in the gene encoding for the cystic fibrosis transmembrane conductance regulator (CFTR) protein which is responsible for fluid and ion transport through epithelial membranes maintaining the formation of a thin slippery mucous layer. CFTR mutations either lead to a trafficking defect where the CFTR protein does not reach the plasma membrane or a gating defect where CFTR protein at the plasma membrane does not function properly. Treatment of cystic fibrosis usually addresses the symptoms to overcome the complications of the disease such as pneumonia, lung infections, pancreatitis, maldigestion and infertility. Vertex pharmaceuticals has been interested in developing small molecules that have the ability to interact with mutated CFTR proteins, aiding in their delivery to the cell membrane and/or restoring their channel function. VX-770 is an orally bioavailable potentiator that has the ability to improve the gating activity and increasing the open probability of CFTR protein in patients carrying the G551D mutation. VX770, Ivacaftor, was recently approved by the US FDA after showing very good improvements in the lung function in CF patients with good safety profile. Our research is focusing on the synthesis of VX770 under mild conditions and formation of labeled derivatives to help in the understanding of its exact mode of action. Different methods were developed toward the synthesis of the two main components, LHS and RHS, of VX770 by using less harsh conditions for a short period of time. We were successfully able to make two photoaffinity labeled derivatives, aryl azide and benzophenone derivatives, which will be beneficial in tracking the drug molecule and revealing the exact site of interaction between the drug and the protein. Synthesis of VX770 fragments was is another focus of interest in our research as they will provide us with information about the best positions for further derivatization.

scholarly journals Cloning and transcriptional regulation of the gene encoding the vacuolar/H+ATPase B subunit ofDictyostelium discoideum

FEBS Letters ◽  
1997 ◽  
Vol 419 (1) ◽  
pp. 37-40 ◽  
Author(s):  
Enrico Bracco ◽  
Barbara Peracino ◽  
Angelika A Noegel ◽  
Salvatore Bozzaro
Keyword(s):  
Transcriptional Regulation ◽  
Gene Encoding ◽  
B Subunit

MID1, a novel Saccharomyces cerevisiae gene encoding a plasma membrane protein, is required for Ca2+ influx and mating

1994 ◽  
Vol 14 (12) ◽  
pp. 8259-8271 ◽  
Author(s):  
H Iida ◽  
H Nakamura ◽  
T Ono ◽  
M S Okumura ◽  
Y Anraku
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Screening Method ◽  
Amino Acid Residues ◽  
Plasma Membrane Protein ◽  
Gene Encoding ◽  
New Gene ◽  
Uptake Activity ◽  
High Concentrations ◽  
Yeast Mutants

By establishing a unique screening method, we have isolated yeast mutants that die only after differentiating into cells with a mating projection, and some of them are also defective in Ca2+ signaling. The mutants were classified into five complementation groups, one of which we studied extensively. This mutation defines a new gene, designated MID1, which encodes an N-glycosylated, integral plasma membrane protein with 548 amino acid residues. The mid1-1 mutant has low Ca2+ uptake activity, loses viability after receiving mating pheromones, and escapes death when incubated with high concentrations of CaCl2. The MID1 gene is nonessential for vegetative growth. The efficiency of mating between MATa mid1-1 and MAT alpha mid1-1 cells is low. These results demonstrate that MID1 is required for Ca2+ influx and mating.

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