AAA+ ATPases: Achieving Diversity of Function with Conserved Machinery

@article{White2007AAAAA,
  title={AAA+ ATPases: Achieving Diversity of Function with Conserved Machinery},
  author={Susan Roehl White and Brett P Lauring},
  journal={Traffic},
  year={2007},
  volume={8}
}
AAA+ adenosine triphosphatases (ATPases) are molecular machines that perform a wide variety of cellular functions. For instance, they can act in vesicle transport, organelle assembly, membrane dynamics and protein unfolding. In most cases, the ATPase domains of these proteins assemble into active ring‐shaped hexamers. As AAA+ proteins have a common structure, a central issue is determining how they use conserved mechanistic principles to accomplish specific biological actions. Here, we review… 
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Assessing heterogeneity in oligomeric AAA+ machines
  • T. Sysoeva
  • Biology, Chemistry
    Cellular and Molecular Life Sciences
  • 2016
TLDR
The first part of this work will provide a broad overview of what arrangements of AAA+ subunits have been structurally observed focusing on diversity of ATPase oligomericEnsembles and heterogeneity within the ensembles.
The molecular principles governing the activity and functional diversity of AAA+ proteins
TLDR
How substrate-bound structures of AAA+ proteins have expanded the understanding of ATP-driven protein remodelling is reviewed, leading to a better understanding of the mechanisms of engagement and processing of their diverse substrates.
Mechanism of protein unfolding and polypeptide translocation by the AAA+ protease ClpXP
TLDR
Strong structural similarities to other ATP-dependent pro-teases, as well as other ring translocases, suggest that the operating principles I havediscerned and describe here may generalize to other biological molecular motors.
Design framework of the MuA remodeling signal that confers preferential complex disassembly by the AAA + unfoldase ClpX by Lorraine Ling
TLDR
A framework is provided to understand the design of recognition signals that specify and target macromolecular complexes to unfolding chaperones and remodelers of the AAA+ superfamily.
Using chemical inhibitors to probe AAA protein conformational dynamics and cellular functions.
ATPase and protease domain movements in the bacterial AAA+ protease FtsH are driven by thermal fluctuations
TLDR
It is suggested that thermal energy, but not chemical energy, provides the major driving force for conformational switching, while ATP, through a state reequilibration, introduces directionality into this process.
A pathway of protein translocation in mitochondria mediated by the AAA-ATPase Bcs1.
ATPase and Protease Domain Movements in the Bacterial AAA+ Protease FtsH Are Driven by Thermal Fluctuations.
Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane
TLDR
The human YME1L protease is a membrane-anchored AAA+ enzyme that controls proteostasis at the inner membrane and intermembrane space of mitochondria and is capable of processively unfolding substrate proteins with substantial thermodynamic stabilities.
Role of AAA(+)-proteins in peroxisome biogenesis and function.
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