Results 21 to 30 of about 9,362,172 (272)

Lysosomal dysfunction in Down syndrome and Alzheimer mouse models is caused by v-ATPase inhibition by Tyr682-phosphorylated APP βCTF

open access: yesScience Advances, 2023
Lysosome dysfunction arises early and propels Alzheimer’s disease (AD). Herein, we show that amyloid precursor protein (APP), linked to early-onset AD in Down syndrome (DS), acts directly via its β-C-terminal fragment (βCTF) to disrupt lysosomal vacuolar
Eunju Im   +9 more
semanticscholar   +1 more source

Endolysosomal impairment by binding of amyloid beta or MAPT/Tau to V-ATPase and rescue via the HYAL-CD44 axis in Alzheimer disease

open access: yesAutophagy, 2023
Impaired activities and abnormally enlarged structures of endolysosomes are frequently observed in Alzheimer disease (AD) brains. However, little is known about whether and how endolysosomal dysregulation is triggered and associated with AD.
Seo-Hyun Kim   +9 more
semanticscholar   +1 more source

Direct control of lysosomal catabolic activity by mTORC1 through regulation of V-ATPase assembly

open access: yesNature Communications, 2022
Mammalian cells can acquire exogenous amino acids through endocytosis and lysosomal catabolism of extracellular proteins. In amino acid-replete environments, nutritional utilization of extracellular proteins is suppressed by the amino acid sensor ...
Edoardo Ratto   +6 more
semanticscholar   +1 more source

The role of individual domains and the significance of shedding of ATP6AP2/(pro)renin receptor in vacuolar H(+)-ATPase biogenesis. [PDF]

open access: yesPLoS ONE, 2013
The ATPase 6 accessory protein 2 (ATP6AP2)/(pro)renin receptor (PRR) is essential for the biogenesis of active vacuolar H(+)-ATPase (V-ATPase). Genetic deletion of ATP6AP2/PRR causes V-ATPase dysfunction and compromises vesicular acidification.
Kenichiro Kinouchi   +12 more
doaj   +1 more source

V-ATPase is a universal regulator of LC3-associated phagocytosis and non-canonical autophagy

open access: yesJournal of Cell Biology, 2022
Hooper et al. report on the role and regulation of V-ATPase in the activation of non-canonical autophagy, including LC3-associated phagocytosis. They reveal new insights into how V-ATPase V0-V1 engagement recruits the autophagy protein ATG16L1 to direct ...
K. Hooper   +6 more
semanticscholar   +1 more source

Neutral sphingomyelinase 2 controls exosome secretion by counteracting V-ATPase-mediated endosome acidification

open access: yesJournal of Cell Science, 2022
During endosome maturation, neutral sphingomyelinase 2 (nSMase2, encoded by SMPD3) is involved in budding of intraluminal vesicles (ILVs) into late endosomes or multivesicular bodies (MVBs).
Dolma Choezom, J. Gross
semanticscholar   +1 more source

Duelling functions of the V-ATPase [PDF]

open access: yesThe EMBO Journal, 2011
The V‐ATPase, the major cellular proton pump, is comprised of the peripheral sector V1 catalysing ATP hydrolysis and the membrane integral sector V0 translocating protons. Ten years ago, Andreas Mayer9s group made the surprising observation that proteolipids of the V0 transmembrane sector are implicated in membrane fusion, but deeper analysis proved to
Scott Cameron C   +2 more
openaire   +4 more sources

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

open access: yesPLoS 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 V-ATPase inhibition by bafilomycin A1

open access: yesNature Communications, 2021
Pharmacological inhibition of vacuolar-type H+-ATPase (V-ATPase) by its specific inhibitor can abrogate tumor metastasis, prevent autophagy, and reduce cellular signaling responses.
Rong Wang   +5 more
semanticscholar   +1 more source

Molecular basis of mEAK7-mediated human V-ATPase regulation

open access: yesNature 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   +3 more
doaj   +1 more source

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