{"title":"与AGC激酶相关的翻译因子和蛋白酶体靶向蛋白复合物的细胞系统生物学","authors":"A. Sobko","doi":"10.37421/1747-0862.2021.15.470","DOIUrl":null,"url":null,"abstract":"Sch-9 appears to be the Saccharomyces cerevisiae homolog of protein kinase B and S6 kinase and is involved in the control of numerous nutrient-sensitive processes, including regulation of cell size, cell cycle progression, and stress resistance. Sch-9 has also been implicated in the regulation of replicative and chronological life span. The availability of data from global studies of protein-protein interactions now makes it possible to predict and validate functional connections between Sch-9, its putative substrates, and other proteins. Sch-9 appears to be involved in control of biosynthetic and catabolic pathways. Thus, the analysis of Sch-9-associated proteins indicates that this kinase may be involved in regulation of protein synthesis. Sch-9 forms a complex with, and, presumably, phosphorylates starvation- and stress-induced protein kinase GCN2, which, in turn, phosphorylates translation initiation factor eIF2-alpha. Sch-9 also interacts with translation factors Arc1, Pab1 and prion-like protein Sup-35. Thus, Sch-9 may be part of the mechanism that relays availability of nutrients to utilization of glucose and to the rates of protein synthesis. One of the interesting outcomes of the proteome-wide analysis of protein-protein interactions in yeast is the finding that Sch-9 associates with Shp1, Cdc48, and Ufd1, which form a complex responsible for the recognition and targeting of ubiquitinated proteins to the proteasome for degradation. It is unknown and remains to be elucidated, whether mammalian paralogues of Sch-9 are also associated with the proteins involved in translation/protein synthesis and proteasomal degradation.","PeriodicalId":88269,"journal":{"name":"Journal of molecular and genetic medicine : an international journal of biomedical research","volume":"15 1","pages":"1-3"},"PeriodicalIF":0.0000,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Cell Systems Biology of Translation Factors and Proteasome-Targeted Protein Complexes Associated with AGC Kinase Sch 9\",\"authors\":\"A. Sobko\",\"doi\":\"10.37421/1747-0862.2021.15.470\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Sch-9 appears to be the Saccharomyces cerevisiae homolog of protein kinase B and S6 kinase and is involved in the control of numerous nutrient-sensitive processes, including regulation of cell size, cell cycle progression, and stress resistance. Sch-9 has also been implicated in the regulation of replicative and chronological life span. The availability of data from global studies of protein-protein interactions now makes it possible to predict and validate functional connections between Sch-9, its putative substrates, and other proteins. Sch-9 appears to be involved in control of biosynthetic and catabolic pathways. Thus, the analysis of Sch-9-associated proteins indicates that this kinase may be involved in regulation of protein synthesis. Sch-9 forms a complex with, and, presumably, phosphorylates starvation- and stress-induced protein kinase GCN2, which, in turn, phosphorylates translation initiation factor eIF2-alpha. Sch-9 also interacts with translation factors Arc1, Pab1 and prion-like protein Sup-35. Thus, Sch-9 may be part of the mechanism that relays availability of nutrients to utilization of glucose and to the rates of protein synthesis. One of the interesting outcomes of the proteome-wide analysis of protein-protein interactions in yeast is the finding that Sch-9 associates with Shp1, Cdc48, and Ufd1, which form a complex responsible for the recognition and targeting of ubiquitinated proteins to the proteasome for degradation. It is unknown and remains to be elucidated, whether mammalian paralogues of Sch-9 are also associated with the proteins involved in translation/protein synthesis and proteasomal degradation.\",\"PeriodicalId\":88269,\"journal\":{\"name\":\"Journal of molecular and genetic medicine : an international journal of biomedical research\",\"volume\":\"15 1\",\"pages\":\"1-3\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2021-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of molecular and genetic medicine : an international journal of biomedical research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.37421/1747-0862.2021.15.470\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of molecular and genetic medicine : an international journal of biomedical research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.37421/1747-0862.2021.15.470","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Cell Systems Biology of Translation Factors and Proteasome-Targeted Protein Complexes Associated with AGC Kinase Sch 9
Sch-9 appears to be the Saccharomyces cerevisiae homolog of protein kinase B and S6 kinase and is involved in the control of numerous nutrient-sensitive processes, including regulation of cell size, cell cycle progression, and stress resistance. Sch-9 has also been implicated in the regulation of replicative and chronological life span. The availability of data from global studies of protein-protein interactions now makes it possible to predict and validate functional connections between Sch-9, its putative substrates, and other proteins. Sch-9 appears to be involved in control of biosynthetic and catabolic pathways. Thus, the analysis of Sch-9-associated proteins indicates that this kinase may be involved in regulation of protein synthesis. Sch-9 forms a complex with, and, presumably, phosphorylates starvation- and stress-induced protein kinase GCN2, which, in turn, phosphorylates translation initiation factor eIF2-alpha. Sch-9 also interacts with translation factors Arc1, Pab1 and prion-like protein Sup-35. Thus, Sch-9 may be part of the mechanism that relays availability of nutrients to utilization of glucose and to the rates of protein synthesis. One of the interesting outcomes of the proteome-wide analysis of protein-protein interactions in yeast is the finding that Sch-9 associates with Shp1, Cdc48, and Ufd1, which form a complex responsible for the recognition and targeting of ubiquitinated proteins to the proteasome for degradation. It is unknown and remains to be elucidated, whether mammalian paralogues of Sch-9 are also associated with the proteins involved in translation/protein synthesis and proteasomal degradation.