Abstract
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.
Highlights
The centrosome apparatus, as its name suggests, has been at the center of cell biology [1, 2]
In 2010, a large scale proteomic study aiming to elucidate the mitotic role of O-GlcNAc transferase (OGT) was carried out [9], and 141 new proteins involved in spindle and cytokinesis were pinpointed to be regulated by O-GlcNAcylation
Since polo-like kinase 1 (PLK1) kinase activity is regulated by phosphorylation at T210 in its kinase domain [16], and T210 is dephosphorylated by the Myosin Phosphatase Targeting Subunit 1 (MYPT1)-Protein Phosphatase 1 cb (PP1cb) complex [17], we investigated MYPT1 O-GlcNAcylation
Summary
The centrosome apparatus, as its name suggests, has been at the center of cell biology [1, 2]. OGT Regulates Centrosomes only writer for the O-GlcNAc modification. It is a possible scenario that some centrosome assembly proteins are under dynamic regulation of both OGT and OGA.
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