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Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder
The nucleolus is essential for ribosome biogenesis and is involved in many other cellular functions. We performed a systematic spatiotemporal dissection of the human nucleolar proteome using confocal microscopy. In total, 1,318 nucleolar proteins were identified; 287 were localized to fibrillar comp...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397901/ https://www.ncbi.nlm.nih.gov/pubmed/32744794 http://dx.doi.org/10.15252/msb.20209469 |
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author | Stenström, Lovisa Mahdessian, Diana Gnann, Christian Cesnik, Anthony J Ouyang, Wei Leonetti, Manuel D Uhlén, Mathias Cuylen‐Haering, Sara Thul, Peter J Lundberg, Emma |
author_facet | Stenström, Lovisa Mahdessian, Diana Gnann, Christian Cesnik, Anthony J Ouyang, Wei Leonetti, Manuel D Uhlén, Mathias Cuylen‐Haering, Sara Thul, Peter J Lundberg, Emma |
author_sort | Stenström, Lovisa |
collection | PubMed |
description | The nucleolus is essential for ribosome biogenesis and is involved in many other cellular functions. We performed a systematic spatiotemporal dissection of the human nucleolar proteome using confocal microscopy. In total, 1,318 nucleolar proteins were identified; 287 were localized to fibrillar components, and 157 were enriched along the nucleoplasmic border, indicating a potential fourth nucleolar subcompartment: the nucleoli rim. We found 65 nucleolar proteins (36 uncharacterized) to relocate to the chromosomal periphery during mitosis. Interestingly, we observed temporal partitioning into two recruitment phenotypes: early (prometaphase) and late (after metaphase), suggesting phase‐specific functions. We further show that the expression of MKI67 is critical for this temporal partitioning. We provide the first proteome‐wide analysis of intrinsic protein disorder for the human nucleolus and show that nucleolar proteins in general, and mitotic chromosome proteins in particular, have significantly higher intrinsic disorder level compared to cytosolic proteins. In summary, this study provides a comprehensive and essential resource of spatiotemporal expression data for the nucleolar proteome as part of the Human Protein Atlas. |
format | Online Article Text |
id | pubmed-7397901 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-73979012020-08-06 Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder Stenström, Lovisa Mahdessian, Diana Gnann, Christian Cesnik, Anthony J Ouyang, Wei Leonetti, Manuel D Uhlén, Mathias Cuylen‐Haering, Sara Thul, Peter J Lundberg, Emma Mol Syst Biol Articles The nucleolus is essential for ribosome biogenesis and is involved in many other cellular functions. We performed a systematic spatiotemporal dissection of the human nucleolar proteome using confocal microscopy. In total, 1,318 nucleolar proteins were identified; 287 were localized to fibrillar components, and 157 were enriched along the nucleoplasmic border, indicating a potential fourth nucleolar subcompartment: the nucleoli rim. We found 65 nucleolar proteins (36 uncharacterized) to relocate to the chromosomal periphery during mitosis. Interestingly, we observed temporal partitioning into two recruitment phenotypes: early (prometaphase) and late (after metaphase), suggesting phase‐specific functions. We further show that the expression of MKI67 is critical for this temporal partitioning. We provide the first proteome‐wide analysis of intrinsic protein disorder for the human nucleolus and show that nucleolar proteins in general, and mitotic chromosome proteins in particular, have significantly higher intrinsic disorder level compared to cytosolic proteins. In summary, this study provides a comprehensive and essential resource of spatiotemporal expression data for the nucleolar proteome as part of the Human Protein Atlas. John Wiley and Sons Inc. 2020-08-03 /pmc/articles/PMC7397901/ /pubmed/32744794 http://dx.doi.org/10.15252/msb.20209469 Text en © 2020 The Authors. Published under the terms of the CC BY 4.0 license This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Stenström, Lovisa Mahdessian, Diana Gnann, Christian Cesnik, Anthony J Ouyang, Wei Leonetti, Manuel D Uhlén, Mathias Cuylen‐Haering, Sara Thul, Peter J Lundberg, Emma Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
title | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
title_full | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
title_fullStr | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
title_full_unstemmed | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
title_short | Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
title_sort | mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397901/ https://www.ncbi.nlm.nih.gov/pubmed/32744794 http://dx.doi.org/10.15252/msb.20209469 |
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