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Updated: Jul 11, 2026
10:39
Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
AAA+ ATPases: achieving diversity of function with conserved machinery
Susan Roehl White1, Brett Lauring1
1Department of Pathology, College of Physicians & Surgeons, Columbia University, New York, NY 10032, USA.
Traffic (Copenhagen, Denmark)
|September 28, 2007
Summary
AAA+ adenosine triphosphatases (ATPases) are crucial molecular machines. Despite diverse functions, they share a common core mechanism, impacting cellular processes and human health.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- AAA+ adenosine triphosphatases (ATPases) are essential molecular machines involved in numerous cellular processes.
- These proteins typically form ring-shaped hexamers, utilizing conserved structural features.
- Understanding how AAA+ proteins achieve diverse functions from a common mechanism is a key scientific question.
Purpose of the Study:
- To review the defining features and motifs of AAA+ domains.
- To describe the cellular activities mediated by various AAA+ proteins.
- To discuss evidence for a common core mechanism across different AAA+ machines.
Main Methods:
- Literature review of AAA+ protein structure and function.
- Analysis of conserved features and motifs within AAA+ domains.
- Synthesis of recent research on AAA+ protein mechanisms.
Main Results:
- AAA+ proteins share common structural elements and motifs.
- Diverse cellular functions, including vesicle transport and protein unfolding, are mediated by AAA+ proteins.
- Evidence suggests a conserved core mechanism underlies the varied activities of AAA+ machines.
Conclusions:
- AAA+ proteins, despite functional diversity, operate via a shared fundamental mechanism.
- This mechanism is critical for cellular function and its disruption leads to genetic diseases.
- Further research into this common mechanism can illuminate AAA+ protein function and disease pathology.
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