Results 41 to 50 of about 147,751 (260)

The Mechanochemistry of V-ATPase Proton Pumps [PDF]

Biophysical Journal, 2000
The vacuolar H(+)-ATPases (V-ATPases) are a universal class of proton pumps that are structurally similar to the F-ATPases. Both protein families are characterized by a membrane-bound segment (V(o), F(o)) responsible for the translocation of protons, and a soluble portion, (V(1), F(1)), which supplies the energy for translocation by hydrolyzing ATP ...
Grabe, Michael, Wang, Hongyun, Oster, George   +2 more
openaire   +2 more sources

The V-ATPases in cancer and cell death

Cancer Gene Therapy, 2022
Transmembrane ATPases are membrane-bound enzyme complexes and ion transporters that can be divided into F-, V-, and A-ATPases according to their structure. The V-ATPases, also known as H+-ATPases, are large multi-subunit protein complexes composed of a peripheral domain (V1) responsible for the hydrolysis of ATP and a membrane-integrated domain (V0 ...
Fangquan Chen, Rui Kang, Jiao Liu, Daolin Tang   +3 more
openaire   +2 more sources

Regulation of V‐ATPases by reversible disassembly [PDF]

FEBS Letters, 2000
V‐ATPases consist of a complex of peripheral subunits containing catalytic sites for ATP hydrolysis, the V1 sector, attached to several membrane subunits containing a proton pore, the V0 sector. ATP‐driven proton transport requires structural and functional coupling of the two sectors, but in vivo, the interaction between the V1 and V0 sectors is ...
openaire   +2 more sources

Rotation of the Proteolipid Ring in the V-ATPase [PDF]

Journal of Biological Chemistry, 2003
V0V1-ATPase is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. We demonstrated recently the rotation of the central stalk subunits in V1, a catalytic sector of V0V1-ATPase (Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M ...
Yokoyama, K. Nakano, M. Imamura, H. Yoshida, M. Tamakoshi, M   +4 more
openaire   +2 more sources

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

FEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura, Shin‐ichi Tate, Kyota Yasuda   +2 more
wiley   +1 more source

Specific V-ATPase expression sub-classifies IDHwt lower-grade gliomas and impacts glioma growth in vivoResearch in context

EBioMedicine, 2019
Background: Cancer cells use specific V-ATPase subunits to activate oncogenic pathways. Therefore, we investigated V-ATPase deregulation in aggressive gliomas and associated signaling.
Andrea Terrasi, Irene Bertolini, Cristina Martelli, Gabriella Gaudioso, Andrea Di Cristofori, Alessandra Maria Storaci, Miriam Formica, Silvano Bosari, Manuela Caroli, Luisa Ottobrini, Thomas Vaccari, Valentina Vaira   +11 more
doaj   +1 more source

An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane

FEBS Letters, EarlyView.
Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa, Akira Hattori, Masafumi Tsujimoto, Toshihide Kobayashi   +3 more
wiley   +1 more source

Dmxl1 Is an Essential Mammalian Gene that Is Required for V-ATPase Assembly and Function In Vivo

Function
The proton pumping V-ATPase drives essential biological processes, such as acidification of intracellular organelles. Critically, the V-ATPase domains, V1 and VO, must assemble to produce a functional holoenzyme.
Amity F Eaton, Elizabeth C Danielson, Diane Capen, Maria Merkulova, Dennis Brown   +4 more
doaj   +1 more source

RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of Organelle Acidification

Frontiers in Cell and Developmental Biology, 2021
The yeast RAVE (Regulator of H+-ATPase of Vacuolar and Endosomal membranes) complex and Rabconnectin-3 complexes of higher eukaryotes regulate acidification of organelles such as lysosomes and endosomes by catalyzing V-ATPase assembly.
Michael C. Jaskolka, Samuel R. Winkley, Patricia M. Kane   +2 more
doaj   +1 more source

Regulation of V-ATPase Assembly in Nutrient Sensing and Function of V-ATPases in Breast Cancer Metastasis [PDF]

Frontiers in Physiology, 2018
V-ATPases are proton pumps that function to acidify intracellular compartments in all eukaryotic cells, and to transport protons across the plasma membrane of certain specialized cells. V-ATPases function in many normal and disease processes, including membrane traffic, protein degradation, pathogen entry, and cancer cell invasion.
Michael P. Collins, Michael Forgac, Michael Forgac   +2 more
openaire   +3 more sources