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J. Biol. Chem., Vol. 278, Issue 20, 18499-18505, May 16, 2003
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From the Department of Biology/Chemistry, Division of Animal
Physiology, University of Osnabrück,
D-49069 Osnabrück, Germany
Primary proton transport by V-ATPases is
regulated via the reversible dissociation of the
V1V0 holoenzyme into its V1
and V0 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 V1 complex detaches from the apical
membrane. Binding studies, however, demonstrated that both the
V1 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 V1
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 C also binds to F-actin. When the
V1 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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AJ519536.
A Novel Role for Subunit C in Mediating Binding of the
H+-V-ATPase to the Actin Cytoskeleton*
*
This work was supported by Deutsche Forschungsgemeinschaft
Grants SFB 431 and GRK 612.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
49-541-9693502; Fax: 49-541-9693503; E-mail:
merzendorfer@biologie.uni-osnabrueck.de.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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