Centrosomes: Til O-GlcNAc Do Us Apart

The centrosome apparatus is vital for spindle assembly and chromosome segregation during mitotic divisions. Its replication, disjunction and separation have to be fine-tuned in space and time. A multitude of post-translational modifications (PTMs) have been implicated in centrosome modulation, inclu...

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Main Authors: Aiyun Yuan, Xiangyan Tang, Jing Li
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-02-01
Series:Frontiers in Endocrinology
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fendo.2020.621888/full
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spelling doaj-3274d2457a3348c1acb2a490881f37d42021-02-01T13:16:57ZengFrontiers Media S.A.Frontiers in Endocrinology1664-23922021-02-011110.3389/fendo.2020.621888621888Centrosomes: Til O-GlcNAc Do Us ApartAiyun YuanXiangyan TangJing LiThe centrosome apparatus is vital for spindle assembly and chromosome segregation during mitotic divisions. Its replication, disjunction and separation have to be fine-tuned in space and time. A multitude of post-translational modifications (PTMs) have been implicated in centrosome modulation, including phosphorylation, ubiquitination and acetylation. Among them is the emerging O-linked N-acetylglucosamine (O-GlcNAc) modification. This quintessential PTM has a sole writer, O-GlcNAc transferase (OGT), and the only eraser, O-GlcNAcase (OGA). O-GlcNAc couples glucose metabolism with signal transduction and forms a yin-yang relationship with phosphorylation. Evidence from proteomic studies as well as single protein investigations has pinpointed a role of O-GlcNAc in centrosome number and separation, centriole number and distribution, as well as the cilia machinery emanating from the centrosomes. Herein we review our current understanding of the sweet modification embedded in centrosome dynamics and speculate that more molecular details will be unveiled in the future.https://www.frontiersin.org/articles/10.3389/fendo.2020.621888/fullO-linked N-acetylglucosamineO-linked N-acetylglucosamine transferasecell cyclecentrosomecilia
collection DOAJ
language English
format Article
sources DOAJ
author Aiyun Yuan
Xiangyan Tang
Jing Li
spellingShingle Aiyun Yuan
Xiangyan Tang
Jing Li
Centrosomes: Til O-GlcNAc Do Us Apart
Frontiers in Endocrinology
O-linked N-acetylglucosamine
O-linked N-acetylglucosamine transferase
cell cycle
centrosome
cilia
author_facet Aiyun Yuan
Xiangyan Tang
Jing Li
author_sort Aiyun Yuan
title Centrosomes: Til O-GlcNAc Do Us Apart
title_short Centrosomes: Til O-GlcNAc Do Us Apart
title_full Centrosomes: Til O-GlcNAc Do Us Apart
title_fullStr Centrosomes: Til O-GlcNAc Do Us Apart
title_full_unstemmed Centrosomes: Til O-GlcNAc Do Us Apart
title_sort centrosomes: til o-glcnac do us apart
publisher Frontiers Media S.A.
series Frontiers in Endocrinology
issn 1664-2392
publishDate 2021-02-01
description The centrosome apparatus is vital for spindle assembly and chromosome segregation during mitotic divisions. Its replication, disjunction and separation have to be fine-tuned in space and time. A multitude of post-translational modifications (PTMs) have been implicated in centrosome modulation, including phosphorylation, ubiquitination and acetylation. Among them is the emerging O-linked N-acetylglucosamine (O-GlcNAc) modification. This quintessential PTM has a sole writer, O-GlcNAc transferase (OGT), and the only eraser, O-GlcNAcase (OGA). O-GlcNAc couples glucose metabolism with signal transduction and forms a yin-yang relationship with phosphorylation. Evidence from proteomic studies as well as single protein investigations has pinpointed a role of O-GlcNAc in centrosome number and separation, centriole number and distribution, as well as the cilia machinery emanating from the centrosomes. Herein we review our current understanding of the sweet modification embedded in centrosome dynamics and speculate that more molecular details will be unveiled in the future.
topic O-linked N-acetylglucosamine
O-linked N-acetylglucosamine transferase
cell cycle
centrosome
cilia
url https://www.frontiersin.org/articles/10.3389/fendo.2020.621888/full
work_keys_str_mv AT aiyunyuan centrosomestiloglcnacdousapart
AT xiangyantang centrosomestiloglcnacdousapart
AT jingli centrosomestiloglcnacdousapart
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