Function and Interactions of Subunit H of the Vacuolar ATPase

Function and Interactions of Subunit H of the Vacuolar ATPase

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The vacuolar H+ ATPase (V-ATPase) is an ATP-driven proton pump. Using a rotary mechanism, the V-ATPase pumps protons from the cytosol to either acidify intracellular compartments or the extracellular space. Employing this simple mechanism, V-ATPases are involved in an array of cellular functions such as receptor-mediated endocytosis, prohormone processing, bone remodeling, and sperm maturation. V-ATPases are large, multi-subunit, two-domain structures. The catalytic V1 domain, composed of subunits A through H, is the site of ATP hydrolysis. The integral domain VO, composed of subunits a, c, c', cq, d, and e, is buried in the membrane and facilitates proton transport. ATP hydrolysis by the V1 domain drives rotation of a rotary complex relative to the stationary part of the enzyme leading to proton translocation through the integral VO domain.The vacuolar H+ ATPase (V-ATPase) is an ATP-driven proton pump. Using a rotary mechanism, the V-ATPase pumps protons from the cytosol to either acidify intracellular compartments or the extracellular space.


Title:Function and Interactions of Subunit H of the Vacuolar ATPase
Author:Kevin C. Jefferies
Publisher:ProQuest - 2008
ISBN-13:

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