Results 1 to 10 of about 147,751 (260)

V-ATPase-dependent induction of selective autophagy [PDF]

Nature Communications
The general consensus is that the vacuolar-type H+-translocating ATPase (V-ATPase) is critical for macroautophagy/autophagy. However, there is a fundamental conundrum because follicular lymphoma-associated mutations in the V-ATPase result in lysosomal ...
Yuxiang Huang, Dimitra Dialynaki, Yuchen Lei, Zhihai Zhang, Charles R. Evans, Daniel J. Klionsky   +5 more
doaj   +2 more sources

V-ATPase Dysfunction in the Brain: Genetic Insights and Therapeutic Opportunities [PDF]

Cells
Vacuolar-type ATPase (v-ATPase) is a multimeric protein complex that regulates H+ transport across membranes and intra-cellular organelle acidification. Catabolic processes, such as endocytic degradation and autophagy, strictly rely on v-ATPase-dependent
Antonio Falace, Greta Volpedo, Marcello Scala, Federico Zara, Pasquale Striano, Anna Fassio   +5 more
doaj   +2 more sources

V-ATPase in cancer: mechanistic insights and therapeutic potentials [PDF]

Cell Communication and Signaling
Vacuolar-type H+-ATPase (V-ATPase) is a crucial proton pump that plays an essential role in maintaining intracellular pH homeostasis and a variety of physiological processes.
Tingting Chen, Xiaotan Lin, Shuo Lu, Bo Li   +3 more
doaj   +2 more sources

V-ATPase in glioma stem cells: a novel metabolic vulnerability [PDF]

Journal of Experimental & Clinical Cancer Research
Background Glioblastoma (GBM) is a lethal brain tumor characterized by the glioma stem cell (GSC) niche. The V-ATPase proton pump has been described as a crucial factor in sustaining GSC viability and tumorigenicity.
Alessandra Maria Storaci, Irene Bertolini, Cristina Martelli, Giorgia De Turris, Nadia Mansour, Mariacristina Crosti, Maria Rosaria De Filippo, Luisa Ottobrini, Luca Valenti, Elisa Polledri, Silvia Fustinoni, Manuela Caroli, Claudia Fanizzi, Silvano Bosari, Stefano Ferrero, Giorgia Zadra, Valentina Vaira   +16 more
doaj   +2 more sources

V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera [PDF]

Insects
Cry2Ab is a significant alternative Bacillus thuringiensis (Bt) protein utilized for managing insect resistance to Cry1 toxins and broadening the insecticidal spectrum of crops containing two or more Bt genes. Unfortunately, the identified receptors fail
Pin Li, Yuge Zhao, Ningbo Zhang, Xue Yao, Xianchun Li, Mengfang Du, Jizhen Wei, Shiheng An   +7 more
doaj   +2 more sources

TBC1D24 interacts with the v-ATPase and regulates intraorganellar pH in neurons [PDF]

iScience
Summary: The vacuolar ATPase (v-ATPase) is essential for acidification of intracellular organelles, including synaptic vesicles. Its activity is controlled by cycles of association and dissociation of the ATP hydrolysis (V1) and proton transport (V0 ...
Sara Pepe, Davide Aprile, Enrico Castroflorio, Antonella Marte, Simone Giubbolini, Samir Hopestone, Anna Parsons, Tânia Soares, Fabio Benfenati, Peter L. Oliver, Anna Fassio   +10 more
doaj   +2 more sources

CLC3 regulates V-ATPase to enhance lysosomal degradation and cisplatin resistance in cervical cancer cells [PDF]

Cell Death Discovery
Chemoresistance remains a major challenge in cervical cancer (CVC) treatment. Lysosomal function, mediated by V-ATPase, is critical in cancer progression and drug resistance. CLC3, a chloride channel that regulates lysosomal acidification, may contribute
Chuyun Chen, Fubin Zhang, Jiayi Shen, Qi Zheng, Zhiyun Zhang, Shun Lu, Lixiao Liu, Tianhong Zhu, Yongming Du, Yutao Guan   +9 more
doaj   +2 more sources

Loss of vacuolar-type H+-ATPase induces caspase-independent necrosis-like death of hair cells in zebrafish neuromasts

Disease Models & Mechanisms, 2021
The vacuolar-type H+-ATPase (V-ATPase) is a multi-subunit proton pump that regulates cellular pH. V-ATPase activity modulates several cellular processes, but cell-type-specific functions remain poorly understood.
Peu Santra, Jeffrey D. Amack
doaj   +1 more source

Probing subunit-subunit interactions in the yeast vacuolar ATPase by peptide arrays. [PDF]

PLoS ONE, 2012
BACKGROUND:Vacuolar (H(+))-ATPase (V-ATPase; V(1)V(o)-ATPase) is a large multisubunit enzyme complex found in the endomembrane system of all eukaryotic cells where its proton pumping action serves to acidify subcellular organelles. In the plasma membrane
Lee S Parsons, Stephan Wilkens
doaj   +1 more source

Molecular basis of mEAK7-mediated human V-ATPase regulation

Nature Communications, 2022
Structural basis of V-ATPase regulation by endogenous proteins is unclear. Here, the authors find mEAK7 as an endogenous V-ATPase modulator and determine its structure with V-ATPase, suggesting the potential role of mEAK7 in V-ATPase regulation.
Rong Wang, Yu Qin, Xiao-Song Xie, Xiaochun Li   +3 more
doaj   +1 more source