Please use this identifier to cite or link to this item:
https://doi.org/10.1371/journal.pgen.1004456
DC Field | Value | |
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dc.title | The Rim15-Endosulfine-PP2ACdc55 Signalling Module Regulates Entry into Gametogenesis and Quiescence via Distinct Mechanisms in Budding Yeast | |
dc.contributor.author | Sarkar S. | |
dc.contributor.author | Dalgaard J.Z. | |
dc.contributor.author | Millar J.B.A. | |
dc.contributor.author | Arumugam P. | |
dc.date.accessioned | 2019-11-08T08:50:16Z | |
dc.date.available | 2019-11-08T08:50:16Z | |
dc.date.issued | 2014 | |
dc.identifier.citation | Sarkar S., Dalgaard J.Z., Millar J.B.A., Arumugam P. (2014). The Rim15-Endosulfine-PP2ACdc55 Signalling Module Regulates Entry into Gametogenesis and Quiescence via Distinct Mechanisms in Budding Yeast. PLoS Genetics 10 (6) : e1004456. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pgen.1004456 | |
dc.identifier.issn | 15537390 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/161950 | |
dc.description.abstract | Quiescence and gametogenesis represent two distinct survival strategies in response to nutrient starvation in budding yeast. Precisely how environmental signals are sensed by yeast cells to trigger quiescence and gametogenesis is not fully understood. A conserved signalling module consisting of Greatwall kinase, Endosulfine and Protein Phosphatase PP2ACdc55 proteins regulates entry into mitosis in Xenopus egg extracts and meiotic maturation in flies. We report here that an analogous signalling module consisting of the serine-threonine kinase Rim15, the Endosulfines Igo1 and Igo2 and the Protein Phosphatase PP2ACdc55, regulates entry into both quiescence and gametogenesis in budding yeast. PP2ACdc55 inhibits entry into gametogenesis and quiescence. Rim15 promotes entry into gametogenesis and quiescence by converting Igo1 into an inhibitor of PP2ACdc55 by phosphorylating at a conserved serine residue. Moreover, we show that the Rim15-Endosulfine-PP2ACdc55 pathway regulates entry into quiescence and gametogenesis by distinct mechanisms. In addition, we show that Igo1 and Igo2 are required for pre-meiotic autophagy but the lack of pre-meiotic autophagy is insufficient to explain the sporulation defect of igo1? igo2? cells. We propose that the Rim15-Endosulfine-PP2ACdc55 signalling module triggers entry into quiescence and gametogenesis by regulating dephosphorylation of distinct substrates. ? 2014 Sarkar et al. | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20191101 | |
dc.subject | Igo1 protein | |
dc.subject | Igo2 protein | |
dc.subject | protein phosphatase PP2A Cdc55 | |
dc.subject | regulator protein | |
dc.subject | Rim15 protein | |
dc.subject | serine | |
dc.subject | unclassified drug | |
dc.subject | cell cycle protein | |
dc.subject | Igo1 protein, S cerevisiae | |
dc.subject | Igo2 protein, S cerevisiae | |
dc.subject | phosphoprotein phosphatase 2 | |
dc.subject | PPH21 protein, S cerevisiae | |
dc.subject | protein kinase | |
dc.subject | Rim15 protein, S cerevisiae | |
dc.subject | Saccharomyces cerevisiae protein | |
dc.subject | article | |
dc.subject | autophagy | |
dc.subject | budding yeast | |
dc.subject | controlled study | |
dc.subject | fungal development | |
dc.subject | gametogenesis | |
dc.subject | nonhuman | |
dc.subject | protein dephosphorylation | |
dc.subject | protein depletion | |
dc.subject | protein expression | |
dc.subject | protein function | |
dc.subject | protein phosphorylation | |
dc.subject | protein protein interaction | |
dc.subject | signal transduction | |
dc.subject | sporogenesis | |
dc.subject | yeast | |
dc.subject | yeast cell | |
dc.subject | gametogenesis | |
dc.subject | genetics | |
dc.subject | growth, development and aging | |
dc.subject | metabolism | |
dc.subject | miosis | |
dc.subject | Saccharomyces cerevisiae | |
dc.subject | Autophagy | |
dc.subject | Cell Cycle Proteins | |
dc.subject | Gametogenesis | |
dc.subject | Miosis | |
dc.subject | Protein Kinases | |
dc.subject | Protein Phosphatase 2 | |
dc.subject | Saccharomyces cerevisiae | |
dc.subject | Saccharomyces cerevisiae Proteins | |
dc.subject | Signal Transduction | |
dc.type | Article | |
dc.contributor.department | BIOLOGICAL SCIENCES | |
dc.description.doi | 10.1371/journal.pgen.1004456 | |
dc.description.sourcetitle | PLoS Genetics | |
dc.description.volume | 10 | |
dc.description.issue | 6 | |
dc.description.page | e1004456 | |
Appears in Collections: | Elements Staff Publications |
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