Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

AAA+ proteins: diversity in function, similarity in structure.

Jamie Snider¹, Walid A Houry

¹Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada, M5S 1A8.

Biochemical Society Transactions

|January 23, 2008

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Insights into the function and structure of the R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1)chaperone complex.

Cell stress & chaperones·2026

Same author

An oncostatin M receptor and chloride intracellular channel 1 crosstalk drives key oncogenic pathways in glioblastoma.

Signal transduction and targeted therapy·2026

Same author

Global mitochondrial connectivity map reveals the landscape of yeast functional assemblies and conserved protein communities.

Nature communications·2026

Same author

An OSMR-CLIC1 cross talk drives key oncogenic pathways in glioblastoma.

bioRxiv : the preprint server for biology·2025

Same author

Small molecule dysregulation of ClpP activity via bidirectional allosteric pathways.

Structure (London, England : 1993)·2025

Same author

Human protein interaction networks of ancestral and variant SARS-CoV-2 in organ-specific cells and bodily fluids.

Nature communications·2025

Same journal

TDP-43 proteinopathy as a biomarker and therapeutic target in amyotrophic lateral sclerosis.

Biochemical Society transactions·2026

Same journal

Advancing the monitoring of organelle contact sites in vitro and in vivo.

Biochemical Society transactions·2026

Same journal

Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.

Biochemical Society transactions·2026

Same journal

Replication associated nuclear DNA mismatch repair across kingdoms.

Biochemical Society transactions·2026

Same journal

Phosphatases of regenerating liver downregulate PTEN to promote tumorigenesis.

Biochemical Society transactions·2026

Same journal

Implications of Rho GTPase signaling in cancer immunotherapy.

Biochemical Society transactions·2026

See all related articles

ATPases associated with various cellular activities (AAA+) proteins are crucial molecular remodelers. This review details their common structures, mechanistic roles, and diverse functions based on recent classifications.

Area of Science:

Molecular Biology
Protein Biochemistry
Evolutionary Biology

Background:

AAA+ proteins are a superfamily within the P-loop NTPase class.
They utilize nucleotide binding and hydrolysis for molecular remodeling.
Despite a common core, AAA+ proteins exhibit diverse functions due to modifications.

Purpose of the Study:

To concisely describe the major structural elements common to all AAA+ proteins.
To explain the mechanistic roles of these structural elements.
To describe the evolutionary and functional diversity of the AAA+ superfamily.

Main Methods:

Review of existing literature on AAA+ protein structure and function.
Analysis of recent classification studies of the AAA+ superfamily.

Related Experiment Videos

Synthesis of information on common structural features and mechanistic principles.

Main Results:

Identification of conserved core architecture in AAA+ proteins.
Description of how sequence and structural modifications lead to functional diversity.
Overview of the mechanistic roles of key structural elements in nucleotide hydrolysis and remodeling.

Conclusions:

AAA+ proteins share a common structural and mechanistic basis for molecular remodeling.
Evolutionary diversification has led to a wide range of functions for this protein superfamily.
Recent classifications aid in understanding the breadth of AAA+ protein roles.