Редактирование: ATP6V1G1

V-type proton ATPase subunit G 1 (V-ATPase subunit G 1) (V-ATPase 13 kDa subunit 1) (Vacuolar proton pump subunit G 1) (Vacuolar proton pump subunit M16) [ATP6G] [ATP6G1] [ATP6J]

==Publications==

{{medline-entry
|title=Chemical screening identifies [[ATM]] as a target for alleviating senescence.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/28346404
|abstract=Senescence, defined as irreversible cell-cycle arrest, is the main driving force of aging and age-related diseases. Here, we performed high-throughput screening to identify compounds that alleviate senescence and identified the ataxia telangiectasia mutated ([[ATM]]) inhibitor KU-60019 as an effective agent. To elucidate the mechanism underlying [[ATM]]'s role in senescence, we performed a yeast two-hybrid screen and found that [[ATM]] interacted with the vacuolar ATPase V  subunits [[ATP6V1E1]] and [[ATP6V1G1]]. Specifically, [[ATM]] decreased E-G dimerization through direct phosphorylation of [[ATP6V1G1]]. Attenuation of [[ATM]] activity restored the dimerization, thus consequently facilitating assembly of the V  and V  domains with concomitant reacidification of the lysosome. In turn, this reacidification induced the functional recovery of the lysosome/autophagy system and was coupled with mitochondrial functional recovery and metabolic reprogramming. Together, our data reveal a new mechanism through which senescence is controlled by the lysosomal-mitochondrial axis, whose function is modulated by the fine-tuning of [[ATM]] activity.
|mesh-terms=* Adenosine Triphosphatases
* Aging
* Animals
* Ataxia Telangiectasia Mutated Proteins
* Cell Nucleus
* Drug Delivery Systems
* Enzyme Activation
* Flow Cytometry
* Humans
* Hydrogen-Ion Concentration
* Lysosomes
* Mice
* Mitochondria
* Morpholines
* Phosphorylation
* Protein Kinase Inhibitors
* Reactive Oxygen Species
* Thioxanthenes

|full-text-url=https://sci-hub.do/10.1038/nchembio.2342
}}
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