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Multiple Ways to Keep FFAT Under Control!
Peroxisomes and the ER are closely inter-connected organelles, which collaborate in the metabolism of lipids. In a recent research paper in the Journal of Cell Biology, we describe a novel mechanism by which peroxisome-ER membrane contact sites are regulated, via phosphorylation of the peroxisomal p...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SAGE Publications
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7612758/ https://www.ncbi.nlm.nih.gov/pubmed/35611050 http://dx.doi.org/10.1177/25152564221101219 |
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author | Kors, Suzan Schrader, Michael Costello, Joseph L. |
author_facet | Kors, Suzan Schrader, Michael Costello, Joseph L. |
author_sort | Kors, Suzan |
collection | PubMed |
description | Peroxisomes and the ER are closely inter-connected organelles, which collaborate in the metabolism of lipids. In a recent research paper in the Journal of Cell Biology, we describe a novel mechanism by which peroxisome-ER membrane contact sites are regulated, via phosphorylation of the peroxisomal protein ACBD5. We found that the interaction between ACBD5 and the ER protein VAPB, which we have previously shown to form a tether complex at peroxisome-ER contacts, is controlled by phosphorylation of ACBD5 at two different sites of its FFAT motif – the VAPB binding site. We also identify the kinase GSK3-β as being responsible for direct phosphorylation of ACBD5 to negatively regulate interaction with VAPB, leading to reduced peroxisome-ER contacts. In this article we provide additional insights into how this work, in combination with other studies on phosphorylation of VAP interactors, suggests a complex system of both positive and negative regulation of the FFAT motif via phosphorylation. |
format | Online Article Text |
id | pubmed-7612758 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | SAGE Publications |
record_format | MEDLINE/PubMed |
spelling | pubmed-76127582022-05-23 Multiple Ways to Keep FFAT Under Control! Kors, Suzan Schrader, Michael Costello, Joseph L. Contact (Thousand Oaks) News and Views Peroxisomes and the ER are closely inter-connected organelles, which collaborate in the metabolism of lipids. In a recent research paper in the Journal of Cell Biology, we describe a novel mechanism by which peroxisome-ER membrane contact sites are regulated, via phosphorylation of the peroxisomal protein ACBD5. We found that the interaction between ACBD5 and the ER protein VAPB, which we have previously shown to form a tether complex at peroxisome-ER contacts, is controlled by phosphorylation of ACBD5 at two different sites of its FFAT motif – the VAPB binding site. We also identify the kinase GSK3-β as being responsible for direct phosphorylation of ACBD5 to negatively regulate interaction with VAPB, leading to reduced peroxisome-ER contacts. In this article we provide additional insights into how this work, in combination with other studies on phosphorylation of VAP interactors, suggests a complex system of both positive and negative regulation of the FFAT motif via phosphorylation. SAGE Publications 2022-05-11 /pmc/articles/PMC7612758/ /pubmed/35611050 http://dx.doi.org/10.1177/25152564221101219 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution 4.0 License (https://creativecommons.org/licenses/by/4.0/) which permits any use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access page (https://us.sagepub.com/en-us/nam/open-access-at-sage). |
spellingShingle | News and Views Kors, Suzan Schrader, Michael Costello, Joseph L. Multiple Ways to Keep FFAT Under Control! |
title | Multiple Ways to Keep FFAT Under Control! |
title_full | Multiple Ways to Keep FFAT Under Control! |
title_fullStr | Multiple Ways to Keep FFAT Under Control! |
title_full_unstemmed | Multiple Ways to Keep FFAT Under Control! |
title_short | Multiple Ways to Keep FFAT Under Control! |
title_sort | multiple ways to keep ffat under control! |
topic | News and Views |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7612758/ https://www.ncbi.nlm.nih.gov/pubmed/35611050 http://dx.doi.org/10.1177/25152564221101219 |
work_keys_str_mv | AT korssuzan multiplewaystokeepffatundercontrol AT schradermichael multiplewaystokeepffatundercontrol AT costellojosephl multiplewaystokeepffatundercontrol |