Interactions between vacuolar H+-ATPases and microfilaments in osteoclasts
Interactions between vacuolar H+-ATPases and microfilaments in osteoclasts
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DOI：
10.1007/s10863-005-9483-y
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发表时间：
2005-12-01
影响因子：
3
通讯作者：
Zuo, J
中科院分区：
文献类型：
--
作者：
Holliday, LS;Bubb, MR;Zuo, J
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 all 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 all 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.
