A novel role for yeast casein kinases in glucose sensing and signaling
Yeasts have sophisticated signaling pathways for sensing glucose, their preferred carbon source, to regulate its uptake and metabolism. One of these is the sensor/receptor-repressor (SRR) pathway, which detects extracellular glucose and transmits an intracellular signal that induces expression of HX...
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Veröffentlicht in: | Molecular biology of the cell 2016-11, Vol.27 (21), p.3369-3375 |
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description | Yeasts have sophisticated signaling pathways for sensing glucose, their preferred carbon source, to regulate its uptake and metabolism. One of these is the sensor/receptor-repressor (SRR) pathway, which detects extracellular glucose and transmits an intracellular signal that induces expression of HXT genes. The yeast casein kinases (Ycks) are key players in this pathway. Our model of the SRR pathway had the Ycks functioning downstream of the glucose sensors, transmitting the signal from the sensors to the Mth1 and Std1 corepressors that are required for repression of HXT gene expression. However, we found that overexpression of Yck1 fails to restore glucose signaling in a glucose sensor mutant. Conversely, overexpression of a glucose sensor suppresses the signaling defect of a yck mutant. These results suggest that the Ycks act upstream or at the level of the glucose sensors. Indeed, we found that the glucose sensor Rgt2 is phosphorylated on Yck consensus sites in its C-terminal tail in a Yck-dependent manner and that this phosphorylation is required for corepressor binding and ultimately HXT expression. This leads to a revised model of the SRR pathway in which the Ycks prime a site on the cytoplasmic tails of the glucose sensors to promote binding of the corepressors. |
doi_str_mv | 10.1091/mbc.e16-05-0342 |
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One of these is the sensor/receptor-repressor (SRR) pathway, which detects extracellular glucose and transmits an intracellular signal that induces expression of HXT genes. The yeast casein kinases (Ycks) are key players in this pathway. Our model of the SRR pathway had the Ycks functioning downstream of the glucose sensors, transmitting the signal from the sensors to the Mth1 and Std1 corepressors that are required for repression of HXT gene expression. However, we found that overexpression of Yck1 fails to restore glucose signaling in a glucose sensor mutant. Conversely, overexpression of a glucose sensor suppresses the signaling defect of a yck mutant. These results suggest that the Ycks act upstream or at the level of the glucose sensors. Indeed, we found that the glucose sensor Rgt2 is phosphorylated on Yck consensus sites in its C-terminal tail in a Yck-dependent manner and that this phosphorylation is required for corepressor binding and ultimately HXT expression. This leads to a revised model of the SRR pathway in which the Ycks prime a site on the cytoplasmic tails of the glucose sensors to promote binding of the corepressors.</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.e16-05-0342</identifier><identifier>PMID: 27630263</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Casein Kinase I - metabolism ; Casein Kinases - metabolism ; DNA-Binding Proteins - metabolism ; Gene Expression Regulation, Fungal - drug effects ; Glucose - metabolism ; Glucose Transport Proteins, Facilitative - metabolism ; Intracellular Signaling Peptides and Proteins - metabolism ; Membrane Proteins - metabolism ; Monosaccharide Transport Proteins - genetics ; Monosaccharide Transport Proteins - metabolism ; Phosphorylation ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; Signal Transduction - drug effects ; Transcription Factors - metabolism</subject><ispartof>Molecular biology of the cell, 2016-11, Vol.27 (21), p.3369-3375</ispartof><rights>2016 Snowdon and Johnston. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).</rights><rights>2016 Snowdon and Johnston. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License ( ). 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-70f03d0a97bcc18cad3625030d83856bd1eaeab512d56913caa6a16c02d37fc23</citedby><cites>FETCH-LOGICAL-c505t-70f03d0a97bcc18cad3625030d83856bd1eaeab512d56913caa6a16c02d37fc23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5170868/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5170868/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27630263$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Fox, Thomas D.</contributor><creatorcontrib>Snowdon, Chris</creatorcontrib><creatorcontrib>Johnston, Mark</creatorcontrib><title>A novel role for yeast casein kinases in glucose sensing and signaling</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>Yeasts have sophisticated signaling pathways for sensing glucose, their preferred carbon source, to regulate its uptake and metabolism. One of these is the sensor/receptor-repressor (SRR) pathway, which detects extracellular glucose and transmits an intracellular signal that induces expression of HXT genes. The yeast casein kinases (Ycks) are key players in this pathway. Our model of the SRR pathway had the Ycks functioning downstream of the glucose sensors, transmitting the signal from the sensors to the Mth1 and Std1 corepressors that are required for repression of HXT gene expression. However, we found that overexpression of Yck1 fails to restore glucose signaling in a glucose sensor mutant. Conversely, overexpression of a glucose sensor suppresses the signaling defect of a yck mutant. These results suggest that the Ycks act upstream or at the level of the glucose sensors. Indeed, we found that the glucose sensor Rgt2 is phosphorylated on Yck consensus sites in its C-terminal tail in a Yck-dependent manner and that this phosphorylation is required for corepressor binding and ultimately HXT expression. 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One of these is the sensor/receptor-repressor (SRR) pathway, which detects extracellular glucose and transmits an intracellular signal that induces expression of HXT genes. The yeast casein kinases (Ycks) are key players in this pathway. Our model of the SRR pathway had the Ycks functioning downstream of the glucose sensors, transmitting the signal from the sensors to the Mth1 and Std1 corepressors that are required for repression of HXT gene expression. However, we found that overexpression of Yck1 fails to restore glucose signaling in a glucose sensor mutant. Conversely, overexpression of a glucose sensor suppresses the signaling defect of a yck mutant. These results suggest that the Ycks act upstream or at the level of the glucose sensors. Indeed, we found that the glucose sensor Rgt2 is phosphorylated on Yck consensus sites in its C-terminal tail in a Yck-dependent manner and that this phosphorylation is required for corepressor binding and ultimately HXT expression. 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subjects | Adaptor Proteins, Signal Transducing - metabolism Casein Kinase I - metabolism Casein Kinases - metabolism DNA-Binding Proteins - metabolism Gene Expression Regulation, Fungal - drug effects Glucose - metabolism Glucose Transport Proteins, Facilitative - metabolism Intracellular Signaling Peptides and Proteins - metabolism Membrane Proteins - metabolism Monosaccharide Transport Proteins - genetics Monosaccharide Transport Proteins - metabolism Phosphorylation Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Signal Transduction - drug effects Transcription Factors - metabolism |
title | A novel role for yeast casein kinases in glucose sensing and signaling |
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