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Cep44 functions in centrosome cohesion by stabilizing rootletin

The centrosome linker serves to hold the duplicated centrosomes together until they separate in late G2/early mitosis. Precisely how the linker is assembled remains an open question. In this study, we identify Cep44 as a novel component of the linker in human cells. Cep44 localizes to the proximal e...

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Autores principales: Hossain, Delowar, Shih, Sunny Y.-P., Xiao, Xintong, White, Julia, Tsang, William Y.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7044459/
https://www.ncbi.nlm.nih.gov/pubmed/31974111
http://dx.doi.org/10.1242/jcs.239616
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author Hossain, Delowar
Shih, Sunny Y.-P.
Xiao, Xintong
White, Julia
Tsang, William Y.
author_facet Hossain, Delowar
Shih, Sunny Y.-P.
Xiao, Xintong
White, Julia
Tsang, William Y.
author_sort Hossain, Delowar
collection PubMed
description The centrosome linker serves to hold the duplicated centrosomes together until they separate in late G2/early mitosis. Precisely how the linker is assembled remains an open question. In this study, we identify Cep44 as a novel component of the linker in human cells. Cep44 localizes to the proximal end of centrioles, including mother and daughter centrioles, and its ablation leads to loss of centrosome cohesion. Cep44 does not impinge on the stability of C-Nap1 (also known as CEP250), LRRC45 or Cep215 (also known as CDK5RAP2), and vice versa, and these proteins are independently recruited to the centrosome. Rather, Cep44 associates with rootletin and regulates its stability and localization to the centrosome. Our findings reveal a role of the previously uncharacterized protein Cep44 for centrosome cohesion and linker assembly.
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spelling pubmed-70444592020-03-12 Cep44 functions in centrosome cohesion by stabilizing rootletin Hossain, Delowar Shih, Sunny Y.-P. Xiao, Xintong White, Julia Tsang, William Y. J Cell Sci Short Report The centrosome linker serves to hold the duplicated centrosomes together until they separate in late G2/early mitosis. Precisely how the linker is assembled remains an open question. In this study, we identify Cep44 as a novel component of the linker in human cells. Cep44 localizes to the proximal end of centrioles, including mother and daughter centrioles, and its ablation leads to loss of centrosome cohesion. Cep44 does not impinge on the stability of C-Nap1 (also known as CEP250), LRRC45 or Cep215 (also known as CDK5RAP2), and vice versa, and these proteins are independently recruited to the centrosome. Rather, Cep44 associates with rootletin and regulates its stability and localization to the centrosome. Our findings reveal a role of the previously uncharacterized protein Cep44 for centrosome cohesion and linker assembly. The Company of Biologists Ltd 2020-02-21 /pmc/articles/PMC7044459/ /pubmed/31974111 http://dx.doi.org/10.1242/jcs.239616 Text en © 2020. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/4.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
spellingShingle Short Report
Hossain, Delowar
Shih, Sunny Y.-P.
Xiao, Xintong
White, Julia
Tsang, William Y.
Cep44 functions in centrosome cohesion by stabilizing rootletin
title Cep44 functions in centrosome cohesion by stabilizing rootletin
title_full Cep44 functions in centrosome cohesion by stabilizing rootletin
title_fullStr Cep44 functions in centrosome cohesion by stabilizing rootletin
title_full_unstemmed Cep44 functions in centrosome cohesion by stabilizing rootletin
title_short Cep44 functions in centrosome cohesion by stabilizing rootletin
title_sort cep44 functions in centrosome cohesion by stabilizing rootletin
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7044459/
https://www.ncbi.nlm.nih.gov/pubmed/31974111
http://dx.doi.org/10.1242/jcs.239616
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