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Allosteric regulation of C. elegans AMP-activated protein kinase

Scanlon, Daniel Michael, Tullet, Jennifer M.A. (2022) Allosteric regulation of C. elegans AMP-activated protein kinase. microPublication Biology, . ISSN 2578-9430. (doi:10.17912/micropub.biology.000534) (KAR id:95705)

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DOI for this version: 10.17912/micropub.biology.000534

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https://doi.org/10.17912/micropub.biology.000534

Abstract

AMP-activated protein kinase (AMPK) is a key metabolic regulator which responds to changes in the AMP:ATP ratio within

cells. In response to high AMP levels, AMPK promotes a metabolic shift towards increased catabolism and autophagy to

restore cellular energy and maintain homeostasis. In C. elegans, AMPK is important for controlling a multitude of functions

including metabolism, reproductive health, and lifespan. AMPK is a heterotrimeric protein consisting of α catalytic, β linker,

and γ regulatory subunits. Active AMPK is characterised by phosphorylation of the α subunit. It is also regulated allosterically

by the nucleotide AMP binding within the γ subunit. C. elegans have five different AMPKγ subunits and their primary amino

acid sequence implies two different modes of AMP-binding. Modifying the ability of AMPKγ to bind adenine nucleotides

could directly impact how effectively AMPK manages energy homeostasis. Despite the importance of the γ subunit, most C.

elegans AMPK research has focused on the catalytic α subunit. Here, we genetically dissect the functional role of the different

γ subunits in relation to physiology and lifespan. We show that in normal animals, three of these γ subunits (aakg-1, aakg-2,

and aakg-3) are required for normal responses to AMP, and contribute to normal fecundity and lifespan.

Item Type: Article
DOI/Identification number: 10.17912/micropub.biology.000534
Uncontrolled keywords: C. elegans, ageing, AMP activated protein kinase
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Jennifer Tullet
Date Deposited: 07 Jul 2022 13:04 UTC
Last Modified: 08 Jul 2022 08:43 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/95705 (The current URI for this page, for reference purposes)
Tullet, Jennifer M.A.: https://orcid.org/0000-0002-2037-526X
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