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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/107063
Actin filaments are involved in the functional coupling of Vo-V1 domains of vacuolar H-ATPase at the Golgi complex
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We previously reported that actin-depolymerizing agents promote the alkalization of the Golgi stack and thetrans-Golgi network. The main determinant of acidic pH at the Golgi is the vacuolar-type H(+)-translocating ATPase (V-ATPase), whose V1domain subunitsBandCbind actin. We have generated a GFP-tagged subunitB2construct (GFP-B2) that is incorporated into the V1domain, which in turn is coupled to the V0sector. GFP-B2 subunit is enriched at distal Golgi compartments in HeLa cells. Subcellular fractionation, immunoprecipitation, and inversal FRAP experiments show that the actin depolymerization promotes the dissociation of V1-V0domains, which entails subunitB2translocation from Golgi membranes to the cytosol. Moreover, molecular interaction between subunitsB2andC1and actin were detected. In addition, Golgi membrane lipid order disruption byd-ceramide-C6 causes Golgi pH alkalization. We conclude that actin regulates the Golgi pH homeostasis maintaining the coupling of V1-V0domains of V-ATPase through the binding of microfilaments to subunitsBandCand preserving the integrity of detergent-resistant membrane organization. These results establish the Golgi-associated V-ATPase activity as the molecular link between actin and the Golgi pH.
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SERRA-PEINADO, Carla, et al. Actin filaments are involved in the functional coupling of Vo-V1 domains of vacuolar H-ATPase at the Golgi complex. Journal of Biological Chemistry. 2016. Vol. 291, num. 14, pags. 7286-7299. ISSN 0021-9258. [consulted: 6 of June of 2026]. Available at: https://hdl.handle.net/2445/107063