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Regulation of lipid droplet turnover by ubiquitin ligases
Mutation of the protein spartin is a cause of one form of spastic paraplegia. Spartin interacts with ubiquitin ligases of the Nedd4 family, and a recent report in BMC Biology now shows that it acts as an adaptor to recruit and activate the ubiquitin ligase AIP4 onto lipid droplets, leading to the ub...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2906420/ https://www.ncbi.nlm.nih.gov/pubmed/20646264 http://dx.doi.org/10.1186/1741-7007-8-94 |
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author | Alberts, Philipp Rotin, Daniela |
author_facet | Alberts, Philipp Rotin, Daniela |
author_sort | Alberts, Philipp |
collection | PubMed |
description | Mutation of the protein spartin is a cause of one form of spastic paraplegia. Spartin interacts with ubiquitin ligases of the Nedd4 family, and a recent report in BMC Biology now shows that it acts as an adaptor to recruit and activate the ubiquitin ligase AIP4 onto lipid droplets, leading to the ubiquitination and degradation of droplet-associated proteins. A deficiency of spartin apparently causes lipid droplets to accumulate. See research article: http://www.biomedcentral.com/1741-7007/8/72/ |
format | Text |
id | pubmed-2906420 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-29064202010-07-20 Regulation of lipid droplet turnover by ubiquitin ligases Alberts, Philipp Rotin, Daniela BMC Biol Commentary Mutation of the protein spartin is a cause of one form of spastic paraplegia. Spartin interacts with ubiquitin ligases of the Nedd4 family, and a recent report in BMC Biology now shows that it acts as an adaptor to recruit and activate the ubiquitin ligase AIP4 onto lipid droplets, leading to the ubiquitination and degradation of droplet-associated proteins. A deficiency of spartin apparently causes lipid droplets to accumulate. See research article: http://www.biomedcentral.com/1741-7007/8/72/ BioMed Central 2010-07-19 /pmc/articles/PMC2906420/ /pubmed/20646264 http://dx.doi.org/10.1186/1741-7007-8-94 Text en Copyright ©2010 Alberts and Rotin; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Commentary Alberts, Philipp Rotin, Daniela Regulation of lipid droplet turnover by ubiquitin ligases |
title | Regulation of lipid droplet turnover by ubiquitin ligases |
title_full | Regulation of lipid droplet turnover by ubiquitin ligases |
title_fullStr | Regulation of lipid droplet turnover by ubiquitin ligases |
title_full_unstemmed | Regulation of lipid droplet turnover by ubiquitin ligases |
title_short | Regulation of lipid droplet turnover by ubiquitin ligases |
title_sort | regulation of lipid droplet turnover by ubiquitin ligases |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2906420/ https://www.ncbi.nlm.nih.gov/pubmed/20646264 http://dx.doi.org/10.1186/1741-7007-8-94 |
work_keys_str_mv | AT albertsphilipp regulationoflipiddropletturnoverbyubiquitinligases AT rotindaniela regulationoflipiddropletturnoverbyubiquitinligases |