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={L S Holliday and Ming Lu and Beth S. M. Lee and R. David Nelson and Suzanne M. Solivan and Li Zhang and Stephen L Gluck},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 41},
  pages={32331-7}
}
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… CONTINUE READING