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J Biol Chem, Vol. 274, Issue 41, 29164-29171, October 8, 1999
,
From the Departments of § Medicine and ¶ Anatomy
and Cell Biology, University of Florida College of Medicine,
Gainesville, Florida 32610 and the Vacuolar H+-ATPases (V-ATPases)
are multisubunit enzymes that acidify compartments of the vacuolar
system of all eukaryotic cells. In osteoclasts, the cells that degrade
bone, V-ATPases, are recruited from intracellular membrane compartments
to the ruffled membrane, a specialized domain of the plasma membrane, where they are maintained at high densities, serving to acidify the
resorption bay at the osteoclast attachment site on bone (Blair, H. C., Teitelbaum, S. L., Ghiselli, R., and Gluck, S. L. (1989) Science 249, 855-857). Here, we describe a new
mechanism involved in controlling the activity of the bone-resorptive
cell. V-ATPase in osteoclasts cultured in vitro was found
to form a detergent-insoluble complex with actin and myosin II through
direct binding of V-ATPase to actin filaments. Plating bone marrow
cells onto dentine slices, a physiologic stimulus that activates
osteoclast resorption, produced a profound change in the association of
the V-ATPase with actin, assayed by coimmunoprecipitation and
immunocytochemical colocalization of actin filaments and V-ATPase in
osteoclasts. Mouse marrow and bovine kidney V-ATPase bound rabbit
muscle F-actin directly with a maximum stoichiometry of 1 mol of
V-ATPase per 8 mol of F-actin and an apparent affinity of 0.05 µM. Electron microscopy of negatively stained samples
confirmed the binding interaction. These findings link transport of
V-ATPase to reorganization of the actin cytoskeleton during osteoclast activation.
Department of
Internal Medicine, Washington University School of Medicine,
St. Louis, Missouri 63110
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