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The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4
The inositol phosphatase, MTMR4 (myotubularin-related protein 4), was identified as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4). hMTMR4 (human MTMR4) and Nedd4 co-immunoprecipitated and co-localized to late endosomes. The PY (Pr...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Portland Press Ltd.
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2657291/ https://www.ncbi.nlm.nih.gov/pubmed/19125695 http://dx.doi.org/10.1042/BJ20081866 |
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author | Plant, Pamela J. Correa, Judy Goldenberg, Neil Bain, James Batt, Jane |
author_facet | Plant, Pamela J. Correa, Judy Goldenberg, Neil Bain, James Batt, Jane |
author_sort | Plant, Pamela J. |
collection | PubMed |
description | The inositol phosphatase, MTMR4 (myotubularin-related protein 4), was identified as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4). hMTMR4 (human MTMR4) and Nedd4 co-immunoprecipitated and co-localized to late endosomes. The PY (Pro-Tyr) motif of hMTMR4 binds to WW (Trp-Trp) domains of hNedd4. MTMR4 expression was decreased in atrophying muscle, whereas Nedd4 expression was increased and hMTMR4 was ubiquitinated by hNedd4, suggesting that this novel interaction may underlie the biological process of muscle breakdown. |
format | Text |
id | pubmed-2657291 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-26572912009-03-30 The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4 Plant, Pamela J. Correa, Judy Goldenberg, Neil Bain, James Batt, Jane Biochem J Accelerated Publication The inositol phosphatase, MTMR4 (myotubularin-related protein 4), was identified as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4). hMTMR4 (human MTMR4) and Nedd4 co-immunoprecipitated and co-localized to late endosomes. The PY (Pro-Tyr) motif of hMTMR4 binds to WW (Trp-Trp) domains of hNedd4. MTMR4 expression was decreased in atrophying muscle, whereas Nedd4 expression was increased and hMTMR4 was ubiquitinated by hNedd4, suggesting that this novel interaction may underlie the biological process of muscle breakdown. Portland Press Ltd. 2009-03-13 2009-04-01 /pmc/articles/PMC2657291/ /pubmed/19125695 http://dx.doi.org/10.1042/BJ20081866 Text en © 2009 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Accelerated Publication Plant, Pamela J. Correa, Judy Goldenberg, Neil Bain, James Batt, Jane The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4 |
title | The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4 |
title_full | The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4 |
title_fullStr | The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4 |
title_full_unstemmed | The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4 |
title_short | The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4 |
title_sort | inositol phosphatase mtmr4 is a novel target of the ubiquitin ligase nedd4 |
topic | Accelerated Publication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2657291/ https://www.ncbi.nlm.nih.gov/pubmed/19125695 http://dx.doi.org/10.1042/BJ20081866 |
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