The Amino-terminal Domain of the B Subunit of Vacuolar H+-ATPase Contains a Filamentous Actin Binding Site*

@article{Holliday2000TheAD,
  title={The Amino-terminal Domain of the B Subunit of Vacuolar H+-ATPase Contains a Filamentous Actin Binding Site*},
  author={Lexie Shannon Holliday and Ming Lu and Beth S. Lee and Raoul D. Nelson and Suzanne M. Solivan and Li Zhang and Stephen L. Gluck},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={32331 - 32337}
}
Vacuolar H+-ATPase (V-ATPase) binds actin filaments with high affinity (K d = 55 nm; Lee, B. S., Gluck, S. L., and Holliday, L. S. (1999) J. Biol. Chem. 274, 29164–29171). We have proposed that this interaction is an important mechanism controlling transport of V-ATPase from the cytoplasm to the plasma membrane of osteoclasts. Here we show that both the B1 (kidney) and B2 (brain) isoforms of the B subunit of V-ATPase contain a microfilament binding site in their amino-terminal domain. In… 
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Vacuolar H+-ATPase Binding to Microfilaments
TLDR
Binding between V-ATPase and F-actin in osteoclasts occurs in response to blocking phosphatidylinositol 3-kinase activity, and this response was fully reversible.
The Amino-terminal Domain of the E Subunit of Vacuolar H+-ATPase (V-ATPase) Interacts with the H Subunit and Is Required for V-ATPase Function*
TLDR
The physiological significance of the interaction between the E and H subunits of V-ATPase is demonstrated and the structure and subunit composition of the central or peripheral stalk of the multisubunit complex is extended to extend previous studies on the arrangement of subunits on the peripheral stalk.
Arabidopsis Vacuolar H+-ATPase (V-ATPase) B Subunits Are Involved in Actin Cytoskeleton Remodeling via Binding to, Bundling, and Stabilizing F-actin*
TLDR
It is demonstrated that AtVABs bind to and co-localize with F-actin, bundle F-Actin to form higher order structures, and stabilize actin filaments in vitro, and these activities were not regulated by calcium.
A Novel Role for Subunit C in Mediating Binding of the H+-V-ATPase to the Actin Cytoskeleton*
TLDR
Overlay blots and co-pelleting assays showed that the recombinant subunit C also binds to F-actin, which may function as an anchor protein regulating the linkage between V-ATPase and the actin-based cytoskeleton.
Actin Filaments Are Involved in the Coupling of V0-V1 Domains of Vacuolar H+-ATPase at the Golgi Complex*
TLDR
It is concluded that actin regulates the Golgi pH homeostasis maintaining the coupling of V1-V0 domains of V-ATPase through the binding of microfilaments to subunits B and C and preserving the integrity of detergent-resistant membrane organization.
Biochemical and functional characterization of the actin-binding activity of the B subunit of yeast vacuolar H+-ATPase
TLDR
The results suggest that actin-binding activity confers on the B subunit of yeast a function that is distinct from its role in the enzymatic activity of the proton pump.
The V-ATPase Subunit C Binds to Polymeric F-actin as Well as to Monomeric G-actin and Induces Cross-linking of Actin Filaments*
TLDR
The interaction of recombinant subunit C with actin is analyzed and it is demonstrated that it binds not only to F-actin but also to monomeric G-Actin, and does not destabilize actin filaments.
Cysteine-mediated Cross-linking Indicates That Subunit C of the V-ATPase Is in Close Proximity to Subunits E and G of the V1 Domain and Subunit a of the V0 Domain*
TLDR
Analysis of photocross-linked products by Western blot reveals that subunit E (part of V1) is in close proximity to both the head domain and foot domain of subunit C, consistent with a role for this subunit in controlling assembly of the V-ATPase complex.
The a-Subunit of the V-type H+-ATPase Interacts with Phosphofructokinase-1 in Humans*
TLDR
Findings indicate a direct link between V-type H+-ATPases and glycolysis via the C-terminal region of the a-subunit of the pump and suggest a novel regulatory mechanism between H+,ATPase function and energy supply.
Characterisation of the human H⁺-ATPase a4 subunit.
TLDR
Findings indicate a direct link between V-ATPase and glycolysis, via the C-terminus of the pump's a subunit, and suggest a novel regulatory mechanismBetween V- ATPase function and energy supply.
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TLDR
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