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| dc.contributor.author | Serra-Peinado, Carla |
|---|---|
| dc.contributor.author | Sicart Casellas, Adrià |
| dc.contributor.author | Llopis, Juan |
| dc.contributor.author | Egea Guri, Gustavo |
| dc.date | 2017-02-16T12:46:14Z |
| dc.date | 2017-02-16T12:46:14Z |
| dc.date | 2016-02-12 |
| dc.date | 2017-02-16T12:46:14Z |
| dc.identifier | 0021-9258 |
| dc.identifier | 658282 |
| dc.identifier | 26872971 |
| dc.identifier.uri | http://hdl.handle.net/2445/107063 |
| dc.description | 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. |
| dc.format | 14 p. |
| dc.format | application/pdf |
| dc.language | eng |
| dc.publisher | American Society for Biochemistry and Molecular Biology |
| dc.relation | Reproducció del document publicat a: https://doi.org/10.1074/jbc.M115.675272 |
| dc.relation | Journal of Biological Chemistry, 2016, vol. 291, num. 14, p. 7286-7299 |
| dc.relation | https://doi.org/10.1074/jbc.M115.675272 |
| dc.rights | (c) American Society for Biochemistry and Molecular Biology, 2016 |
| dc.rights | info:eu-repo/semantics/openAccess |
| dc.subject | Aparell de Golgi |
| dc.subject | Citosquelet |
| dc.subject | Proteïnes citosquelètiques |
| dc.subject | Enzimologia |
| dc.subject | Homeòstasi |
| dc.subject | Golgi apparatus |
| dc.subject | Cytoskeleton |
| dc.subject | Cytoskeletal proteins |
| dc.subject | Enzymology |
| dc.subject | Homeostasis |
| dc.title | Actin filaments are involved in the functional coupling of Vo-V1 domains of vacuolar H-ATPase at the Golgi complex |
| dc.type | info:eu-repo/semantics/article |
| dc.type | info:eu-repo/semantics/publishedVersion |
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