ArticleThe Journal of cell biology2016
Cell cycle-dependent phosphorylation of Sec4p controls membrane deposition during cytokinesis.
Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- In-depth and 3-dimensional exploration of the budding yeast phosphoproteome.EMBO reports · 2021Article
- Phosphorylation of Rab GTPases in the regulation of membrane trafficking.Traffic (Copenhagen, Denmark) · 2020Article
- Extensive GTPase crosstalk regulates Golgi trafficking and maturation.Current opinion in cell biology · 2020Review
- Review
- Regulation of Exocyst Function in Pollen Tube Growth by Phosphorylation of Exocyst Subunit EXO70C2.Frontiers in plant science · 2020Article
- Functions and regulation of the Polo-like kinase Cdc5 in the absence and presence of DNA damage.Current genetics · 2018Review
- Polarized Exocytosis.Cold Spring Harbor perspectives in biology · 2017Review
- Distinct roles of the polarity factors Boi1 and Boi2 in the control of exocytosis and abscission in budding yeast.Molecular biology of the cell · 2017Article
- Nine unanswered questions about cytokinesis.The Journal of cell biology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Intracellular trafficking is an essential and conserved eukaryotic process. Rab GTPases are a family of proteins that regulate and provide specificity for discrete membrane trafficking steps by harnessing a nucleotide-bound cycle. Global proteomic screens have revealed many Rab GTPases as phosphoproteins, but the effects of this modification are not well understood. Using the Saccharomyces cerevisiae Rab GTPase Sec4p as a model, we have found that phosphorylation negatively regulates Sec4p function by disrupting the interaction with the exocyst complex via Sec15p. We demonstrate that phosphorylation of Sec4p is a cell cycle-dependent process associated with cytokinesis. Through a genomic kinase screen, we have also identified the polo-like kinase Cdc5p as a positive regulator of Sec4p phosphorylation. Sec4p spatially and temporally localizes with Cdc5p exclusively when Sec4p phosphorylation levels peak during the cell cycle, indicating Sec4p is a direct Cdc5p substrate. Our data suggest the physiological relevance of Sec4p phosphorylation is to facilitate the coordination of membrane-trafficking events during cytokinesis.
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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.