Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Stenström, Lovisa, Mahdessian, Diana, Gnann, Christian, Cesnik, Anthony J, Ouyang, Wei, Leonetti, Manuel D, Uhlén, Mathias, Cuylen‐Haering, Sara, Thul, Peter J, Lundberg, Emma
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
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
_version_ 1783565853637214208
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
work_keys_str_mv AT stenstromlovisa mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT mahdessiandiana mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT gnannchristian mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT cesnikanthonyj mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT ouyangwei mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT leonettimanueld mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT uhlenmathias mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT cuylenhaeringsara mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT thulpeterj mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder
AT lundbergemma mappingthenucleolarproteomerevealsaspatiotemporalorganizationrelatedtointrinsicproteindisorder