The Role of AAA+ Proteins in Protein Repair and Degradation

214.3K

views

66

authors

22

articles

The Role of AAA+ Proteins in Protein Repair and Degradation

214.3K

views

66

authors

22

articles

Editorial

02 October 2018

Editorial: The Role of AAA+ Proteins in Protein Repair and Degradation

James Shorter

and

Walid A. Houry

12,658 views

18 citations

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2

University of Toronto

University of Pennsylvania

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ATPases Associated with diverse cellular Activities (AAA+) is a superfamily of proteins that carry out a large variety of functions essential to cell physiology, including control of protein homeostasis, DNA replication, recombination, chromatin remodeling, ribosomal RNA processing, molecular targeting, organelle biogenesis, and membrane fusion. Members of this superfamily are defined by the presence of what is termed the AAA+ domain containing the canonical Walker A and B motifs required for ATP binding and hydrolysis. They typically form hexameric complexes and act as motors to remodel other proteins, DNA/RNA, or multicomponent complexes. Indeed, many chaperones and ATP-dependent proteases are or have subunits that belong to this superfamily.

There has been substantial progress in identifying the structure and mechanism of function of a large number of AAA+ proteins. In this series, a detailed structural and biochemical view is provided of several AAA+ chaperones and proteases, namely: ClpXP, ClpAPS, ClpB and Hsp104, FtsH, 19S proteasome, Lon, p97, Pex1/6, CbbQ, torsin, and NSF.

Contributors are encouraged to submit perspectives, reviews, and original research articles.

ATPases Associated with diverse cellular Activities (AAA+) is a superfamily of proteins that carry out a large variety of functions essential to cell physiology, including control of protein homeostasis, DNA replication, recombination, chromatin remodeling, ribosomal RNA processing, molecular targeting, organelle biogenesis, and membrane fusion. Members of this superfamily are defined by the presence of what is termed the AAA+ domain containing the canonical Walker A and B motifs required for ATP binding and hydrolysis. They typically form hexameric complexes and act as motors to remodel other proteins, DNA/RNA, or multicomponent complexes. Indeed, many chaperones and ATP-dependent proteases are or have subunits that belong to this superfamily.

There has been substantial progress in identifying the structure and mechanism of function of a large number of AAA+ proteins. In this series, a detailed structural and biochemical view is provided of several AAA+ chaperones and proteases, namely: ClpXP, ClpAPS, ClpB and Hsp104, FtsH, 19S proteasome, Lon, p97, Pex1/6, CbbQ, torsin, and NSF.

Contributors are encouraged to submit perspectives, reviews, and original research articles.

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University of Toronto

University of Pennsylvania

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Frontiers in Molecular Biosciences

Structural Biology, Protein Folding, Misfolding and Degradation

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Frontiers in Cell and Developmental Biology

Structural Biology

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