ArticleJournal of cell science2013
Phosphorylation of Chs2p regulates interaction with COPII.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Mechanisms of COPII coat assembly and cargo recognition in the secretory pathway.Nature reviews. Molecular cell biology · 2025Review
- The N-terminal disordered region of ChsB regulates its efficient transport to the hyphal apical surface in Aspergillus nidulans.Current genetics · 2023Article
- Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022Review
- PP2A-Cdc55 phosphatase regulates actomyosin ring contraction and septum formation during cytokinesis.Cellular and molecular life sciences : CMLS · 2022Article
- Review
- Protease dead separase inhibits chromosome segregation and RAB-11 vesicle trafficking.Cell cycle (Georgetown, Tex.) · 2017Article
- Mechanisms of Cytokinesis in Basidiomycetous Yeasts.Fungal biology reviews · 2017Article
- Actomyosin ring driven cytokinesis in budding yeast.Seminars in cell & developmental biology · 2016Review
- Ingression Progression Complexes Control Extracellular Matrix Remodelling during Cytokinesis in Budding Yeast.PLoS genetics · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Trafficking of the chitin synthase Chs2p from the endoplasmic reticulum (ER) to the bud-neck in late mitosis is tightly regulated by the cell cycle via phosphorylation of serine residues in the N-terminus of the protein. Here, we describe the effects of Chs2p phosphorylation on the interaction with coat protein complex II (COPII). Identification of a cdc5(ts) mutant, which fails to transport Chs2p-3xGFP to the bud-neck and instead accumulates the protein in intracellular puncta, led us to discover that Chs2p-3xGFP accumulates at ER exit sites in metaphase-arrested wild-type cells. Using an in vitro ER vesicle formation assay we showed that phosphorylation of Chs2p by the cyclin-dependent kinase CDK1 prevents packaging into COPII vesicles, whereas dephosphorylation of Chs2p by the phosphatase Cdc14p stimulates selection into the vesicles. We found that the cytoplasmic N-terminal domain of Chs2p, which contains the CDK1 phosphorylation sites, interacts with the COPII component Sec24p in a yeast two-hybrid assay and that phosphomimetic substitutions of serines at the CDK1 consensus sites reduces the interaction. Our data suggest that dephosphorylation functions as a molecular switch for regulated ER exit of Chs2p.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.