Results 51 to 60 of about 10,440,305 (287)

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

CryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7

Life Science Alliance, 2022
The structure of mammalian V-ATPase with mEAK-7 shows how a TLDc domain-containing protein can bind the proton pump to form an activity-sensitive interaction.
Yong Zi Tan, Yazan M Abbas, Jing Ze Wu, Di Wu, Kristine A Keon, Geoffrey G Hesketh, Stephanie A Bueler, Anne-Claude Gingras, Carol V Robinson, Sergio Grinstein, John L Rubinstein   +10 more
doaj   +1 more source

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

Autolysosome biogenesis and developmental senescence are regulated by both Spns1 and v-ATPase

, 2016
Spns1 (Spinster homolog 1 [Drosophila]) in vertebrates, as well as Spin (Spinster) in Drosophila, is a hypothetical lysosomal H+-carbohydrate transporter, which functions at a late stage of macroautophagy (hereafter autophagy).
Shuji Kishi (53191), Alam Khan (3357497), Andrew V. Samuelson (546579), Daniel J. Klionsky (53548), Shanshan Lian (116699), Tomoyuki Sasaki (589298), Jesse R. Llop (546576), Wenbiao Chen (665650)   +7 more
core   +1 more source

V-ATPase controls tumor growth and autophagy in a Drosophila model of gliomagenesis

, 2021
Glioblastoma (GBM), a very aggressive and incurable tumor, often results from constitutive activation of EGFR (epidermal growth factor receptor) and of phosphoinositide 3-kinase (PI3K).
Formica, Miriam, Knævelsrud, Helene, Bertolini, Irene, Carminati, Francesca, Storaci, Alessandra Maria, Vaira, Valentina, Vaccari, Thomas, Helene Knævelsrud, Valentina Vaira, Thomas Vaccari, Alessandra Maria Storaci, Miriam Formica, Irene Bertolini, Francesca Carminati   +13 more
core   +1 more source

Emerging experimental and computational methods for studying redox‐regulated structural transitions

FEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass, Dana Reichmann, Gábor Erdős   +2 more
wiley   +1 more source

Synergistic perspectives—How single‐molecule biophysics complement biochemical understanding

FEBS Letters, EarlyView.
In this review, we discuss how ensemble biochemistry and single‐molecule approaches are complementary, outline commonly used single‐molecule techniques, and illustrate their relevance through two representative case studies: chromatin organization by SMC complexes and pathway choice during DNA double‐strand break repair.
Sara De Bragança, Eline L. Jansen, Jorine M. Eeftens   +2 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