Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
M Forgac - Nature reviews Molecular cell biology, 2007 - nature.com
The acidity of intracellular compartments and the extracellular environment is crucial to
various cellular processes, including membrane trafficking, protein degradation, bone …
various cellular processes, including membrane trafficking, protein degradation, bone …
The V-type H+ ATPase: molecular structure and function,physiological roles and regulation
KW Beyenbach, H Wieczorek - Journal of Experimental …, 2006 - journals.biologists.com
It was nearly 30 years before the V-type H+ ATPase was admitted to the small circle of bona
fide transport ATPases alongside F-type and P-type ATPases. The V-type H+ ATPase is an …
fide transport ATPases alongside F-type and P-type ATPases. The V-type H+ ATPase is an …
Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
J Zhao, S Benlekbir, JL Rubinstein - Nature, 2015 - nature.com
Abstract Eukaryotic vacuolar H+-ATPases (V-ATPases) are rotary enzymes that use energy
from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of …
from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of …
[HTML][HTML] Diversification of the type IV filament superfamily into machines for adhesion, protein secretion, DNA uptake, and motility
Processes of molecular innovation require tinkering and shifting in the function of existing
genes. How this occurs in terms of molecular evolution at long evolutionary scales remains …
genes. How this occurs in terms of molecular evolution at long evolutionary scales remains …
Regulation and isoform function of the V-ATPases
M Toei, R Saum, M Forgac - Biochemistry, 2010 - ACS Publications
The vacuolar (H+)-ATPases are ATP-dependent proton pumps that acidify intracellular
compartments and, in some cases, transport protons across the plasma membrane of …
compartments and, in some cases, transport protons across the plasma membrane of …
The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase
PM Kane - Microbiology and Molecular Biology Reviews, 2006 - Am Soc Microbiol
All eukaryotic cells contain multiple acidic organelles, and V-ATPases are central players in
organelle acidification. Not only is the structure of V-ATPases highly conserved among …
organelle acidification. Not only is the structure of V-ATPases highly conserved among …
Renal Vacuolar H+-ATPase
Vacuolar H+-ATPases are ubiquitous multisubunit complexes mediating the ATP-dependent
transport of protons. In addition to their role in acidifying the lumen of various intracellular …
transport of protons. In addition to their role in acidifying the lumen of various intracellular …
Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding
The ability of electrospray to propel large viruses into a mass spectrometer is established
and is rationalized by analogy to the atmospheric transmission of the common cold. Much …
and is rationalized by analogy to the atmospheric transmission of the common cold. Much …
[HTML][HTML] Eukaryotic V-ATPase: novel structural findings and functional insights
V Marshansky, JL Rubinstein, G Grüber - Biochimica et Biophysica Acta …, 2014 - Elsevier
The eukaryotic V-type adenosine triphosphatase (V-ATPase) is a multi-subunit membrane
protein complex that is evolutionarily related to F-type adenosine triphosphate (ATP) …
protein complex that is evolutionarily related to F-type adenosine triphosphate (ATP) …
Structure of the Rotor of the V-Type Na+-ATPase from Enterococcus hirae
T Murata, I Yamato, Y Kakinuma, AGW Leslie… - Science, 2005 - science.org
The membrane rotor ring from the vacuolar-type (V-type) sodium ion–pumping adenosine
triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which …
triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which …