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AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1

The AMP-activated protein kinase (AMPK) is known to maintain the integrity of cellular mitochondrial networks by (i) promoting fission, (ii) inhibiting fusion, (iii) promoting recycling of damaged components via mitophagy, (iv) enhancing lysosomal biogenesis to support mitophagy, and (v) promoting b...

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Detalles Bibliográficos
Autores principales: Freemantle, Jordana B, Hardie, D Grahame
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10445941/
https://www.ncbi.nlm.nih.gov/pubmed/37621729
http://dx.doi.org/10.1093/lifemeta/load027
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author Freemantle, Jordana B
Hardie, D Grahame
author_facet Freemantle, Jordana B
Hardie, D Grahame
author_sort Freemantle, Jordana B
collection PubMed
description The AMP-activated protein kinase (AMPK) is known to maintain the integrity of cellular mitochondrial networks by (i) promoting fission, (ii) inhibiting fusion, (iii) promoting recycling of damaged components via mitophagy, (iv) enhancing lysosomal biogenesis to support mitophagy, and (v) promoting biogenesis of new mitochondrial components. While the AMPK targets underlying the first three of these effects are known, a recent paper suggests that direct phosphorylation of the folliculin-interacting protein 1 (FNIP1) by AMPK may be involved in the remaining two.
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spelling pubmed-104459412023-08-24 AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1 Freemantle, Jordana B Hardie, D Grahame Life Metab Research Highlight The AMP-activated protein kinase (AMPK) is known to maintain the integrity of cellular mitochondrial networks by (i) promoting fission, (ii) inhibiting fusion, (iii) promoting recycling of damaged components via mitophagy, (iv) enhancing lysosomal biogenesis to support mitophagy, and (v) promoting biogenesis of new mitochondrial components. While the AMPK targets underlying the first three of these effects are known, a recent paper suggests that direct phosphorylation of the folliculin-interacting protein 1 (FNIP1) by AMPK may be involved in the remaining two. Oxford University Press 2023-06-22 /pmc/articles/PMC10445941/ /pubmed/37621729 http://dx.doi.org/10.1093/lifemeta/load027 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of Higher Education Press. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Highlight
Freemantle, Jordana B
Hardie, D Grahame
AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1
title AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1
title_full AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1
title_fullStr AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1
title_full_unstemmed AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1
title_short AMPK promotes lysosomal and mitochondrial biogenesis via folliculin:FNIP1
title_sort ampk promotes lysosomal and mitochondrial biogenesis via folliculin:fnip1
topic Research Highlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10445941/
https://www.ncbi.nlm.nih.gov/pubmed/37621729
http://dx.doi.org/10.1093/lifemeta/load027
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