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Article

A conserved inter-domain communication mechanism regulates the ATPase activity of the AAA-protein Drg1.

Scientific reports - 17 Mar 2017

Prattes Michael, Loibl Mathias, Zisser Gertrude, Luschnig Daniel, Kappel Lisa, Rössler Ingrid, Grassegger Manuela, Hromic Altijana, Krieger Elmar, Gruber Karl, Pertschy Brigitte, Bergler Helmut

Abstract excerpt

AAA-ATPases fulfil essential roles in different cellular pathways and often act in form of hexameric complexes. Interaction with pathway-specific substrate and adaptor proteins recruits them to their targets and modulates their catalytic activity. This substrate dependent regulation of ATP hydrolysis in the AAA-domains is mediated by a non-catalytic N-terminal domain. The exact mechanisms that transmit the signal...

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Share to Adenosine Triphosphatases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 28303975
DOI: 10.1038/srep44751
PMCID: PMC5356007

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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