Stimulus-induced phosphorylation of vacuolar H+-ATPase by protein kinase a

DC FieldValueLanguage
dc.contributor.authorVoss, Martin
dc.contributor.authorVitavska, Olga
dc.contributor.authorWalz, Bernd
dc.contributor.authorWieczorek, Helmut
dc.contributor.authorBaumann, Otto
dc.date.accessioned2021-12-23T16:07:19Z-
dc.date.available2021-12-23T16:07:19Z-
dc.date.issued2007
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/7816-
dc.description.abstractEukaryotic vacuolar-type H+-ATPases (V-ATPases) are regulated by the reversible disassembly of the active V1V0 holoenzyme into a cytosolic V-1 complex and a membrane-bound V-0 complex. The signaling cascades that trigger these events in response to changing cellular conditions are largely unknown. We report that the V-1 subunit C of the tobacco hornworm Manduca sexta interacts with protein kinase A and is the only V-ATPase subunit that is phosphorylated by protein kinase A. Subunit C can be phosphorylated as single polypeptide as well as a part of the V-1 complex but not as a part of the V1V0 holoenzyme. Both the phosphorylated and the unphosphorylated form of subunit C are able to reassociate with the V-1 complex from which subunit C had been removed before. Using salivary glands of the blowfly Calliphora vicina in which V-ATPase reassembly and activity is regulated by the neurohormone serotonin via protein kinase A, we show that the membrane-permeable cAMP analog 8-(4-chlorophenylthio) adenosine-3', 5'-cyclic monophosphate (8-CPT-cAMP) causes phosphorylation of subunit C in a tissue homogenate and that phosphorylation is reduced by incubation with antibodies against subunit C. Similarly, incubation of intact salivary glands with 8-CPT-cAMP or serotonin leads to the phosphorylation of subunit C, but this is abolished by H-89, an inhibitor of protein kinase A. These data suggest that subunit C binds to and serves as a substrate for protein kinase A and that this phosphorylation may be a regulatory switch for the formation of the active V1V0 holoenzyme.
dc.language.isoen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.relation.ispartofJOURNAL OF BIOLOGICAL CHEMISTRY
dc.subjectBiochemistry & Molecular Biology
dc.subjectBLOWFLY CALLIPHORA-VICINA
dc.subjectBONE-RESORPTION
dc.subjectCYCLIC-AMP
dc.subjectDROSOPHILA-MELANOGASTER
dc.subjectMALPIGHIAN TUBULES
dc.subjectPLASMA-MEMBRANE
dc.subjectPROTON PUMP
dc.subjectSALIVARY-GLANDS
dc.subjectSUBUNIT-C
dc.subjectV-ATPASE
dc.titleStimulus-induced phosphorylation of vacuolar H+-ATPase by protein kinase a
dc.typejournal article
dc.identifier.doi10.1074/jbc.M703368200
dc.identifier.isiISI:000250840200055
dc.description.volume282
dc.description.issue46
dc.description.startpage33735
dc.description.endpage33742
dc.identifier.eissn1083351X
dc.publisher.place9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
dcterms.isPartOf.abbreviationJ. Biol. Chem.
dcterms.oaStatushybrid
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidViOl437-
crisitem.author.netidWiHe990-
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