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10.1074/jbc.M115.675272

http://scihub22266oqcxt.onion/10.1074/jbc.M115.675272
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suck abstract from ncbi


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pmid26872971
      J+Biol+Chem 2016 ; 291 (14 ): 7286-99
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  • Actin Filaments Are Involved in the Coupling of V0-V1 Domains of Vacuolar H+-ATPase at the Golgi Complex #MMPMID26872971
  • Serra-Peinado C ; Sicart A ; Llopis J ; Egea G
  • J Biol Chem 2016[Apr]; 291 (14 ): 7286-99 PMID26872971 show ga
  • 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.
  • |Actin Cytoskeleton/genetics/*metabolism [MESH]
  • |Cytosol/enzymology [MESH]
  • |Golgi Apparatus/*enzymology/genetics [MESH]
  • |HeLa Cells [MESH]
  • |Humans [MESH]
  • |Hydrogen-Ion Concentration [MESH]
  • |Intracellular Membranes/*enzymology [MESH]
  • |Protein Structure, Tertiary [MESH]


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