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First published online May 15, 2009
Journal of Experimental Biology 212, 1604-1610 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.025866

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Review Article

The little we know on the structure and machinery of V-ATPase

Shai Saroussi and Nathan Nelson^*

Biochemistry Department, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel

^* Author for correspondence (e-mail: nelson{at}post.tau.ac.il)

Accepted 21 January 2009

The life of every eukaryotic cell depends on the function of vacuolar H⁺-ATPase (V-ATPase). Today we know that V-ATPase is vital for many more physiological and biochemical processes than it was expected three decades ago when the enzyme was discovered. These range from a crucial role in the function of internal organelles such as vacuoles, lysosomes, synaptic vesicles, endosomes, secretory granules and the Golgi apparatus to the plasma membrane of several organisms and specific tissues, and specialized cells. The overall structure and mechanism of action of the V-ATPase is supposed to be similar to that of the well-characterized F-type ATP synthase (F-ATPase). Both consist of a soluble catalytic domain (V₁ or F₁) that is coupled to a membrane-spanning domain (V_o or F_o) by one or more `stalk' components. Owing to the complexity and challenging properties of V-ATPase its study is lagging behind that of its relative F-ATPase. Time will tell whether V-ATPase shares an identical mechanism of action with F-ATPase or its mode of operation is unique.

Key words: V-ATPase, secretory pathway, membrane proteins, mechanism of action, structure

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