The study of vacuolar-type ATPases by single particle electron microscopy

Biochem Cell Biol. 2014 Dec;92(6):460-6. doi: 10.1139/bcb-2014-0086. Epub 2014 Sep 3.


Nature's molecular machines often work through the concerted action of many different protein subunits, which can give rise to large structures with complex activities. Vacuolar-type ATPases (V-ATPases) are membrane-embedded protein assemblies with a unique rotary catalytic mechanism. The dynamic nature and instability of V-ATPases make structural and functional studies of these enzymes challenging. Electron microscopy (EM) techniques, especially single particle electron cryomicroscopy (cryo-EM) and negative-stain EM, have provided extensive insight into the structure and function of these protein complexes. This minireview outlines what has been learned about V-ATPases using electron microscopy, highlights current challenges for their structural study, and discusses what cryo-EM will allow us to learn about these fascinating enzymes in the future.

Keywords: ATPase de type vacuolaire; V-ATPase; cryo-EM; cryo-ME; cryomicroscopie électronique; electron cryomicroscopy; electron microscopy; microscopie électronique; vacuolar-type ATPase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cryoelectron Microscopy / methods*
  • Humans
  • Vacuolar Proton-Translocating ATPases / ultrastructure*


  • Vacuolar Proton-Translocating ATPases