A novel role for subunit C in mediating binding of the H+-V-ATPase to the actin cytoskeleton
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Vitavska, O | |
dc.contributor.author | Wieczorek, H | |
dc.contributor.author | Merzendorfer, H | |
dc.date.accessioned | 2021-12-23T16:02:44Z | - |
dc.date.available | 2021-12-23T16:02:44Z | - |
dc.date.issued | 2003 | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/5580 | - |
dc.description.abstract | Primary proton transport by V-ATPases is regulated via the reversible dissociation of the V1V0 holoenzyme into its V-1 and V-0 subcomplexes. Laser scanning microscopy of different tissues from the tobacco hornworm revealed co-localization of the holoenzyme and F-actin close to the apical membranes of the epithelial cells. In midgut goblet cells, no co-localization was observed under conditions where the V-1 complex detaches from the apical membrane. Binding studies, however, demonstrated that both the V-1 complex and the holoenzyme interact with F-actin, the latter with an apparently higher affinity. To identify F-actin binding subunits, we performed overlay blots that revealed two V-1 subunits as binding partners, namely subunit B, resembling the situation in the osteoclast V-ATPase (Holliday, L. S., Lu, M., Lee, B. S., Nelson, R. D., Solivan, S., Zhang, L., and Gluck, S. L. (2000) J. Biol. Chem. 275, 32331-32337), but, in addition, subunit C, which gets released during reversible dissociation of the holoenzyme. Overlay blots and co-pelleting assays showed that the recombinant subunit Calso binds to F-actin. When the V-1 complex was reconstituted with recombinant subunit C, enhanced binding to F-actin was observed. Thus, subunit C may function as an anchor protein regulating the linkage between V-ATPase and the actin-based cytoskeleton. | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | ANIMAL PLASMA-MEMBRANE | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CLATHRIN | |
dc.subject | DISSOCIATION | |
dc.subject | IN-VIVO | |
dc.subject | ION-TRANSPORT | |
dc.subject | PROTON PUMP | |
dc.subject | PURIFICATION | |
dc.subject | TOBACCO HORNWORM MIDGUT | |
dc.subject | TRANSPORTING EPITHELIA | |
dc.subject | VACUOLAR-TYPE ATPASE | |
dc.title | A novel role for subunit C in mediating binding of the H+-V-ATPase to the actin cytoskeleton | |
dc.type | journal article | |
dc.identifier.doi | 10.1074/jbc.M212844200 | |
dc.identifier.isi | ISI:000182838300119 | |
dc.description.volume | 278 | |
dc.description.issue | 20 | |
dc.description.startpage | 18499 | |
dc.description.endpage | 18505 | |
dc.publisher.place | 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
dcterms.oaStatus | hybrid | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | ViOl437 | - |
crisitem.author.netid | WiHe990 | - |
crisitem.author.netid | MeHa731 | - |
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geprüft am 23.05.2024