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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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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. |
format | Online Article Text |
id | pubmed-10445941 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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