Phosphorylation is one of the major posttranslational modifications to control plant growth and development.Opaque2(O2)represents a central hub for endosperm filling,which largely determines seed yield and nutrient st...Phosphorylation is one of the major posttranslational modifications to control plant growth and development.Opaque2(O2)represents a central hub for endosperm filling,which largely determines seed yield and nutrient storage in maize.However,it still remains unclear how O2 phosphorylation orchestrates endosperm filling and nutrient quality.Here,we systematically identified the phosphorylation sites of O2 during endosperm filling.A total of 18 phosphorylation sites were found in O2 and five sites were identified to apparently modulate its subcellular localization and transactivation capacity.In addition,a conserved protein kinase CK1 was confirmed to interact with and phosphorylate O2 at the residue Threonine(T)202 to promote O2-mediated transactivation and protein stability.Overexpression of CK1 resulted in increased kernel size,100-kernel weight and nutrient storage.Phosphorylation-mimic O2 seeds at T202 exhibited enhanced kernel dimension,test weight,vitreous endosperm area and nutrient accumulation,whereas the phosphorylation-deficient O2 seeds did not.Collectively,this study establishes a comprehensive phosphocode atlas of O2 during endosperm filling and highlights the importance of phosphorylation modification in O2 to precisely orchestrate maize yield and nutrient quality.展开更多
Male infertility constitutes a major global public health concern,with the underlying etiology remaining unidentified in nearly half of the diagnosed cases.Protein kinase CK1α(CK1α)functions as a pivotal regulator o...Male infertility constitutes a major global public health concern,with the underlying etiology remaining unidentified in nearly half of the diagnosed cases.Protein kinase CK1α(CK1α)functions as a pivotal regulator of cell cycle progression,pre-mRNA processing,and spliceosome-associated pathways through interactions with specific splicing factors.Comprehensive analyses revealed CK1αexpression in both germ cells and somatic cells of mouse testes,implicating its involvement in spermatogenic regulation.However,the physiological roles and mechanistic basis of CK1αfunction in Sertoli cells remain unclear.In this study,CK1αwas highly expressed in Sertoli cells,and conditional knockout of CK1αin murine Sertoli cells induced profound testicular atrophy and complete infertility.This phenotype was characterized by rapid depletion of Sertoli cells and spermatogenic dysfunction.Subsequent analyses demonstrated that CK1αregulated the fate determination of fetal and neonatal Sertoli cells in mice.At the molecular level,CK1αpromoted Sertoli cell survival through interaction with the splicing factor ZRSR1 to modulate apoptosis.Collectively,these findings establish CK1αas a key regulator of alternative splicing and male reproduction,providing critical insights into the molecular mechanisms underlying testicular development and reproductive function.展开更多
Casein kinase 1α(CK1α) mediates the phosphorylation and degradation of interferon-α/β receptor 1(IFNAR1) in response to viral infection. However, how CK1α regulates hepatitis B virus(HBV) replication and the anti...Casein kinase 1α(CK1α) mediates the phosphorylation and degradation of interferon-α/β receptor 1(IFNAR1) in response to viral infection. However, how CK1α regulates hepatitis B virus(HBV) replication and the anti-HBV effects of IFN-α are less reported. Here we show that CK1α can interact with IFNAR1 in hepatoma carcinoma cells and increased the abundance of IFNAR1 by reducing the ubiquitination levels in the presence of HBV.Furthermore, CK1α promotes the IFN-α triggered JAK-STAT signaling pathway and consequently enhances the antiviral effects of IFN-α against HBV replication. Our results collectively provide evidence that CK1α positively regulates the anti-HBV activity of IFN-α in hepatoma carcinoma cells, which would be a promising therapeutic target to improve the effectiveness of IFN-α therapy to cure CHB.展开更多
基金supported by Biological Breeding-National Science and Technology Major Project(2023ZD04069)Young Scientist Project(2023YFD1200008)+2 种基金the National Natural Science Foundation of China(32472122)Sichuan Provincial General Project(24NSFSC1704)the Open Project Program and Biological Breeding Program of State Key Laboratory of Crop Gene Exploration and Utilization in Southwest China(SKL-ZY202211).
文摘Phosphorylation is one of the major posttranslational modifications to control plant growth and development.Opaque2(O2)represents a central hub for endosperm filling,which largely determines seed yield and nutrient storage in maize.However,it still remains unclear how O2 phosphorylation orchestrates endosperm filling and nutrient quality.Here,we systematically identified the phosphorylation sites of O2 during endosperm filling.A total of 18 phosphorylation sites were found in O2 and five sites were identified to apparently modulate its subcellular localization and transactivation capacity.In addition,a conserved protein kinase CK1 was confirmed to interact with and phosphorylate O2 at the residue Threonine(T)202 to promote O2-mediated transactivation and protein stability.Overexpression of CK1 resulted in increased kernel size,100-kernel weight and nutrient storage.Phosphorylation-mimic O2 seeds at T202 exhibited enhanced kernel dimension,test weight,vitreous endosperm area and nutrient accumulation,whereas the phosphorylation-deficient O2 seeds did not.Collectively,this study establishes a comprehensive phosphocode atlas of O2 during endosperm filling and highlights the importance of phosphorylation modification in O2 to precisely orchestrate maize yield and nutrient quality.
基金supported by the National Natural Science Foundation of China(32130098)。
文摘Male infertility constitutes a major global public health concern,with the underlying etiology remaining unidentified in nearly half of the diagnosed cases.Protein kinase CK1α(CK1α)functions as a pivotal regulator of cell cycle progression,pre-mRNA processing,and spliceosome-associated pathways through interactions with specific splicing factors.Comprehensive analyses revealed CK1αexpression in both germ cells and somatic cells of mouse testes,implicating its involvement in spermatogenic regulation.However,the physiological roles and mechanistic basis of CK1αfunction in Sertoli cells remain unclear.In this study,CK1αwas highly expressed in Sertoli cells,and conditional knockout of CK1αin murine Sertoli cells induced profound testicular atrophy and complete infertility.This phenotype was characterized by rapid depletion of Sertoli cells and spermatogenic dysfunction.Subsequent analyses demonstrated that CK1αregulated the fate determination of fetal and neonatal Sertoli cells in mice.At the molecular level,CK1αpromoted Sertoli cell survival through interaction with the splicing factor ZRSR1 to modulate apoptosis.Collectively,these findings establish CK1αas a key regulator of alternative splicing and male reproduction,providing critical insights into the molecular mechanisms underlying testicular development and reproductive function.
基金supported by the National Key Research and Development Program of China(2018YFE0107500)the Natural Science Foundation Project of Science and Technology Agency of Chongqing YuZhong District(20200122)to Hu Yuana Natural Science Foundation Project of CQ CSTC(cstc2021jcyj-msxmX0276)to Chen YanMeng
文摘Casein kinase 1α(CK1α) mediates the phosphorylation and degradation of interferon-α/β receptor 1(IFNAR1) in response to viral infection. However, how CK1α regulates hepatitis B virus(HBV) replication and the anti-HBV effects of IFN-α are less reported. Here we show that CK1α can interact with IFNAR1 in hepatoma carcinoma cells and increased the abundance of IFNAR1 by reducing the ubiquitination levels in the presence of HBV.Furthermore, CK1α promotes the IFN-α triggered JAK-STAT signaling pathway and consequently enhances the antiviral effects of IFN-α against HBV replication. Our results collectively provide evidence that CK1α positively regulates the anti-HBV activity of IFN-α in hepatoma carcinoma cells, which would be a promising therapeutic target to improve the effectiveness of IFN-α therapy to cure CHB.
