Introduction of ATP6V0C
V-type proton ATPase 16 kDa proteolipid subunit (ATP6V0C) is encoded by ATP6V0C gene, which is mapped to chromosome 16p13.3. ATP6V0C is the bafilomycin A1-binding subunit of vacuolar ATPase (V-ATPase), an enzyme complex that critically regulates the eukaryotic intracellular organelles acidification. V-ATPase is organized into two coordinately operating multi-subunit domains: a peripheral V1 domain where ATP hydrolysis provides energy for proton movement, and an integral membrane V0 domain where proton translocation takes place. ATP6V0C is the c subunit of the V0 domain. ATP6V0C is most abundant in brain and kidney.
|Basic Information of ATP6V0C|
|Protein Name||V-type proton ATPase 16 kDa proteolipid subunit|
|Aliases||Vacuolar proton pump 16 kDa proteolipid subunit|
|Organism||Homo sapiens (Human)|
Function of ATP6V0C Membrane Protein
Localized to many different membranes of eukaryotic cells including lysosomes, endosomes, Golgi-derived vesicles, ANF secretory vesicles, V-ATPase has well documented functions, including vesicle fusion with vacuoles and the acidification of eukaryotic intracellular organelles, that is essential for many intracellular processes, such as protein sorting, zymogen activation, synaptic vesicle proton gradient generation, and receptor-mediated endocytosis. ATP6V0C acts as a part of the proton channel of V-ATPases and is indispensable for the V-ATPase assembly and functions. It has been shown that ATP6V0C knockdown can inhibit vesicular acidification and sensitize cells to stress-induced cell death. In addition, knockdown of ATP6V0C in neuronal cells is shown to adversely affect autophagy-lysosome pathway function and cause the abnormal accumulation of ALP-associated substrates including α-syn and APP-CTFs, suggesting the relevance of ATP6V0C to age-related neurodegenerative disease. ATP6V0C can be degraded via the ubiquitin-proteasome pathway after being ubiquitinated by RNF182.
Fig.1 The predicted structure of ATP6V0C. (Bienert, 2017)
Application of ATP6V0C Membrane Protein in Literature
This article indicates that ATP6V0C may be associated with keeping constitutive and stress-induced alkaline phosphatase function, in particular, the metabolism of substrates which accumulate in age-related neurodegenerative disease. Additionally, it may be associated with disease pathogenesis.
This article finds that siRNA knockdown of ATP6V0C leads to almost complete loss of infectious virus production, suggesting that an HCMV microRNA can target a critical cellular factor required for virus replication.
This article suggests that a novel regulator of HIF-1alpha, ATP6V0C, regulates HIF-1alpha expression by bafilomycin.
This article confirms that a novel brain-enriched RING finger E3 ligase interacts with ATP6V0C protein, suggesting that it may have an influence in controlling the turnover of an essential component of neurotransmitter release machinery.
This article indicates that ATP6V0C regulates dopamine release from gene-transferred striatal cells of parkinsonian mice and from nerve terminals in the striatum of dopamine neurons of normal mice, suggesting that it may be helpful as a rescue molecule in addition to endogenous dopamine synthetic enzymes in the gene therapy of Parkinson's disease.
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