Vacuolar H+-ATPases (V-ATPases) are transported from cytosolic compartments to the ruffled plasma membrane of osteoclasts as they activate to resorb bone. Transport of V-ATPases is essential for bone resorption, and is associated with binding interactions between V-ATPases and microfilaments that are mediated by an actin-binding site in subunit B. This site is contained within 44 amino acids in the amino terminal domain, and requires a sequence motif that resembles an actin-binding motif found in mammalian profilin 1. Small alterations in the profilin-like sequence disrupt the actin-binding activity of subunit B. The interaction between V-ATPases and microfilaments in osteoclasts is regulated in response to changes in phosphatidylinositol-3 kinase activity. During internalization of V-ATPases from the plasma membrane of osteoclasts after a cycle of resorption, V-ATPases bind microfilaments that are in podosomes, dynamic actin-based structures, also present in metastatic cancer cells. Studies are ongoing to establish the physiological role of the microfilament-binding activity of subunit B in osteoclasts and in other cells.
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Holliday, L.S., Bubb, M.R., Jiang, J. et al. Interactions Between Vacuolar H+-ATPases and Microfilaments in Osteoclasts. J Bioenerg Biomembr 37, 419–423 (2005). https://doi.org/10.1007/s10863-005-9483-y
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DOI: https://doi.org/10.1007/s10863-005-9483-y