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FMRP attenuates activity dependent modifications in the mitochondrial proteome

Homeostatic plasticity is necessary for the construction and maintenance of functional neuronal networks, but principal molecular mechanisms required for or modified by homeostatic plasticity are not well understood. We recently reported that homeostatic plasticity induced by activity deprivation is...

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Autores principales: Bülow, Pernille, Zlatic, Stephanie A., Wenner, Peter A., Bassell, Gary J., Faundez, Victor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8086361/
https://www.ncbi.nlm.nih.gov/pubmed/33931071
http://dx.doi.org/10.1186/s13041-021-00783-w
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author Bülow, Pernille
Zlatic, Stephanie A.
Wenner, Peter A.
Bassell, Gary J.
Faundez, Victor
author_facet Bülow, Pernille
Zlatic, Stephanie A.
Wenner, Peter A.
Bassell, Gary J.
Faundez, Victor
author_sort Bülow, Pernille
collection PubMed
description Homeostatic plasticity is necessary for the construction and maintenance of functional neuronal networks, but principal molecular mechanisms required for or modified by homeostatic plasticity are not well understood. We recently reported that homeostatic plasticity induced by activity deprivation is dysregulated in cortical neurons from Fragile X Mental Retardation protein (FMRP) knockout mice (Bulow et al. in Cell Rep 26: 1378-1388 e1373, 2019). These findings led us to hypothesize that identifying proteins sensitive to activity deprivation and/or FMRP expression could reveal pathways required for or modified by homeostatic plasticity. Here, we report an unbiased quantitative mass spectrometry used to quantify steady-state proteome changes following chronic activity deprivation in wild type and Fmr1(−/y) cortical neurons. Proteome hits responsive to both activity deprivation and the Fmr1(−/y) genotype were significantly annotated to mitochondria. We found an increased number of mitochondria annotated proteins whose expression was sensitive to activity deprivation in Fmr1(−/y) cortical neurons as compared to wild type neurons. These findings support a novel role of FMRP in attenuating mitochondrial proteome modifications induced by activity deprivation. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13041-021-00783-w.
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spelling pubmed-80863612021-04-30 FMRP attenuates activity dependent modifications in the mitochondrial proteome Bülow, Pernille Zlatic, Stephanie A. Wenner, Peter A. Bassell, Gary J. Faundez, Victor Mol Brain Research Homeostatic plasticity is necessary for the construction and maintenance of functional neuronal networks, but principal molecular mechanisms required for or modified by homeostatic plasticity are not well understood. We recently reported that homeostatic plasticity induced by activity deprivation is dysregulated in cortical neurons from Fragile X Mental Retardation protein (FMRP) knockout mice (Bulow et al. in Cell Rep 26: 1378-1388 e1373, 2019). These findings led us to hypothesize that identifying proteins sensitive to activity deprivation and/or FMRP expression could reveal pathways required for or modified by homeostatic plasticity. Here, we report an unbiased quantitative mass spectrometry used to quantify steady-state proteome changes following chronic activity deprivation in wild type and Fmr1(−/y) cortical neurons. Proteome hits responsive to both activity deprivation and the Fmr1(−/y) genotype were significantly annotated to mitochondria. We found an increased number of mitochondria annotated proteins whose expression was sensitive to activity deprivation in Fmr1(−/y) cortical neurons as compared to wild type neurons. These findings support a novel role of FMRP in attenuating mitochondrial proteome modifications induced by activity deprivation. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13041-021-00783-w. BioMed Central 2021-04-30 /pmc/articles/PMC8086361/ /pubmed/33931071 http://dx.doi.org/10.1186/s13041-021-00783-w Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research
Bülow, Pernille
Zlatic, Stephanie A.
Wenner, Peter A.
Bassell, Gary J.
Faundez, Victor
FMRP attenuates activity dependent modifications in the mitochondrial proteome
title FMRP attenuates activity dependent modifications in the mitochondrial proteome
title_full FMRP attenuates activity dependent modifications in the mitochondrial proteome
title_fullStr FMRP attenuates activity dependent modifications in the mitochondrial proteome
title_full_unstemmed FMRP attenuates activity dependent modifications in the mitochondrial proteome
title_short FMRP attenuates activity dependent modifications in the mitochondrial proteome
title_sort fmrp attenuates activity dependent modifications in the mitochondrial proteome
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8086361/
https://www.ncbi.nlm.nih.gov/pubmed/33931071
http://dx.doi.org/10.1186/s13041-021-00783-w
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