ArticleCell reports2022
Mitotic phosphorylation inhibits the Golgi mannosidase MAN1A1.
Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Organelle-specific regulation of ferroptosis.Biology direct · 2026Review
- MGAT1-Guided complex N-Glycans on CD73 regulate immune evasion in triple-negative breast cancer.Nature communications · 2025Article
- Baseline unfolded protein response signaling adjusts the timing of the mammalian cell cycle.Molecular biology of the cell · 2024Article
- Golgi defect as a major contributor to lysosomal dysfunction.Frontiers in cell and developmental biology · 2024Review
- The Cyclin-dependent kinase 1: more than a cell cycle regulator.British journal of cancer · 2023Review
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
N-glycans are processed mainly in the Golgi, and a well-organized Golgi structure is required for accurate glycosylation. However, during mitosis the Golgi undergoes severe fragmentation. The resulting trafficking block leads to an extended exposure of cargo molecules to Golgi enzymes. It is unclear how cells avoid glycosylation defects during mitosis. In this study, we report that Golgi α-1,2-mannosidase IA (MAN1A1), the first enzyme that cargo proteins encounter once arriving the Golgi, is phosphorylated at serine 12 by CDK1 in mitosis, which attenuates its activity, affects the production of glycan isomers, and reduces its interaction with the subsequent glycosyltransferase, MGAT1. Expression of wild-type MAN1A1, but not its phosphomimetic mutant, rescues the glycosylation defects in mannosidase I-deficient cells, whereas expression of its phosphorylation-deficient mutant in mitosis increases the formation of complex glycans. Our study reveals that glycosylation is regulated by cytosolic signaling during the cell cycle.
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