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New insights into subcomplex assembly and modifications of centrosomal proteins

This review provides a brief overview of the recent work on centrosome proteomics, protein complex identification and functional characterization with an emphasis on the literature of the last three years. Proteomics, genetic screens and comparative genomics studies in different model organisms have...

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Autores principales: Habermann, Karin, Lange, Bodo MH
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3479078/
https://www.ncbi.nlm.nih.gov/pubmed/22800182
http://dx.doi.org/10.1186/1747-1028-7-17
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author Habermann, Karin
Lange, Bodo MH
author_facet Habermann, Karin
Lange, Bodo MH
author_sort Habermann, Karin
collection PubMed
description This review provides a brief overview of the recent work on centrosome proteomics, protein complex identification and functional characterization with an emphasis on the literature of the last three years. Proteomics, genetic screens and comparative genomics studies in different model organisms have almost exhaustively identified the molecular components of the centrosome. However, much knowledge is still missing on the protein-protein interactions, protein modifications and molecular changes the centrosome undergoes throughout the cell cycle and development. The dynamic nature of this large multi-protein complex is reflected in the variety of annotated subcellular locations and biological processes of its proposed components. Some centrosomal proteins and complexes have been studied intensively in different organisms and provided detailed insight into centrosome functions. For example, the molecular, structural and functional characterization of the γ-Tubulin ring complex (γ-TuRC) and the the discovery of the Augmin/HAUS complex has advanced our understanding of microtubule (MT) capture, nucleation and organization. Surprising findings revealed new functions and localizations of proteins that were previously regarded as bona fide centriolar or centrosome components, e.g. at the kinetochore or in the nuclear pore complex regulating MT plus end capture or mRNA processing. Many centrosome components undergo posttranslational modifications such as phosphorylation, SUMOylation and ubiquitylation that are critical in modulating centrosome function and biology. A wealth of information has recently become available driven by new developments in technologies such as mass spectrometry, light and electron microscopy providing more detailed molecular and structural definition of the centrosome and particular roles of proteins throughout the cell cycle and development.
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spelling pubmed-34790782012-10-24 New insights into subcomplex assembly and modifications of centrosomal proteins Habermann, Karin Lange, Bodo MH Cell Div Review This review provides a brief overview of the recent work on centrosome proteomics, protein complex identification and functional characterization with an emphasis on the literature of the last three years. Proteomics, genetic screens and comparative genomics studies in different model organisms have almost exhaustively identified the molecular components of the centrosome. However, much knowledge is still missing on the protein-protein interactions, protein modifications and molecular changes the centrosome undergoes throughout the cell cycle and development. The dynamic nature of this large multi-protein complex is reflected in the variety of annotated subcellular locations and biological processes of its proposed components. Some centrosomal proteins and complexes have been studied intensively in different organisms and provided detailed insight into centrosome functions. For example, the molecular, structural and functional characterization of the γ-Tubulin ring complex (γ-TuRC) and the the discovery of the Augmin/HAUS complex has advanced our understanding of microtubule (MT) capture, nucleation and organization. Surprising findings revealed new functions and localizations of proteins that were previously regarded as bona fide centriolar or centrosome components, e.g. at the kinetochore or in the nuclear pore complex regulating MT plus end capture or mRNA processing. Many centrosome components undergo posttranslational modifications such as phosphorylation, SUMOylation and ubiquitylation that are critical in modulating centrosome function and biology. A wealth of information has recently become available driven by new developments in technologies such as mass spectrometry, light and electron microscopy providing more detailed molecular and structural definition of the centrosome and particular roles of proteins throughout the cell cycle and development. BioMed Central 2012-07-16 /pmc/articles/PMC3479078/ /pubmed/22800182 http://dx.doi.org/10.1186/1747-1028-7-17 Text en Copyright ©2012 Habermann and Lange; 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 Review
Habermann, Karin
Lange, Bodo MH
New insights into subcomplex assembly and modifications of centrosomal proteins
title New insights into subcomplex assembly and modifications of centrosomal proteins
title_full New insights into subcomplex assembly and modifications of centrosomal proteins
title_fullStr New insights into subcomplex assembly and modifications of centrosomal proteins
title_full_unstemmed New insights into subcomplex assembly and modifications of centrosomal proteins
title_short New insights into subcomplex assembly and modifications of centrosomal proteins
title_sort new insights into subcomplex assembly and modifications of centrosomal proteins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3479078/
https://www.ncbi.nlm.nih.gov/pubmed/22800182
http://dx.doi.org/10.1186/1747-1028-7-17
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