1. Aims and scope Sciences in Cold and Arid Regions （SCAR） is a bimonthly journal that publishes in English the latest research achievements in processes and the patterns of the Earth surface system in cold and ari...1. Aims and scope Sciences in Cold and Arid Regions （SCAR） is a bimonthly journal that publishes in English the latest research achievements in processes and the patterns of the Earth surface system in cold and arid regions. Researches in cold regions emphasize particularly on the cold-region-characterized physical, chemical and biological processes and their interactions, and on the response of cryosphere to global change and human aclivities as well as their effects on envirolmaent and the acclimatizable strategies; focus on the objects of glacier, snow,展开更多
Dear Editor, Plants have evolved elaborate mechanisms by which cell elongation regulation is coupled to the environmental signals. The plasma membrane receptor kinase FERONIA （FER） has emerged as an important regula...Dear Editor, Plants have evolved elaborate mechanisms by which cell elongation regulation is coupled to the environmental signals. The plasma membrane receptor kinase FERONIA （FER） has emerged as an important regulatory node in controlling cell elongation and hormone crosstalk （Guo et al., 2009; Deslauriers and Larsen, 2010; Duan et al., 2010; Yu et al.,展开更多
The endoplasmic reticulum-associated degradation （ERAD） is a highly conserved mechanism to remove mis- folded membrane/secretory proteins from the endoplasmic reticulum （ER）. While many of the individual component...The endoplasmic reticulum-associated degradation （ERAD） is a highly conserved mechanism to remove mis- folded membrane/secretory proteins from the endoplasmic reticulum （ER）. While many of the individual components of the ERAD machinery are well characterized in yeast and mammals, our knowledge of a plant ERAD process is rather limited. Here, we report a functional study of an Arabidopsis homolog （AtOS9） of an ER luminal lectin Yos9 （OS-9 in mammals） that recognizes a unique asparagine-linked glycan on misfolded proteins. We discovered that AtOS9 is an ER-Iocalized glyco- protein that is co-expressed with many known/predicted ER chaperones. AT-DNA insertional atos9-t mutation blocks the degradation of a structurally imperfect yet biochemically competent brassinosteroid （BR） receptor bril-9, causing its increased accumulation in the ER and its consequent leakage to the cell surface responsible for restoring the BR sensitivity and suppressing the dwarfism of the bril-9 mutant. In addition, we identified a missense mutation in AtOS9 in a recently discovered ERAD mutant ems-rnutagenized bril suppressor 6 （ebs6-1）. Moreover, we showed that atos9-t also inhibits the ERAD of bril-5, another ER-retained BR receptor, and a misfolded EFR, a BRIl-like receptor for the bacterial translation elongation factor EF-Tu. Furthermore, we found that AtOS9 interacted biochemically and genetically with EBS5, an Arabidopsis homolog of the yeast Hrd3/mammalian SellL known to collaborate with Yos9/OS-9 to select ERAD clients. Taken together, our results demonstrated a functional role of AtOS9 in a plant ERAD process that degrades misfolded receptor-like kinases.展开更多
文摘1. Aims and scope Sciences in Cold and Arid Regions （SCAR） is a bimonthly journal that publishes in English the latest research achievements in processes and the patterns of the Earth surface system in cold and arid regions. Researches in cold regions emphasize particularly on the cold-region-characterized physical, chemical and biological processes and their interactions, and on the response of cryosphere to global change and human aclivities as well as their effects on envirolmaent and the acclimatizable strategies; focus on the objects of glacier, snow,
文摘Dear Editor, Plants have evolved elaborate mechanisms by which cell elongation regulation is coupled to the environmental signals. The plasma membrane receptor kinase FERONIA （FER） has emerged as an important regulatory node in controlling cell elongation and hormone crosstalk （Guo et al., 2009; Deslauriers and Larsen, 2010; Duan et al., 2010; Yu et al.,
基金This work was partly supported by grants from National Institutes of Health （GM060519） and National Science Foundation （IOS 1121496） to J.L.
文摘The endoplasmic reticulum-associated degradation （ERAD） is a highly conserved mechanism to remove mis- folded membrane/secretory proteins from the endoplasmic reticulum （ER）. While many of the individual components of the ERAD machinery are well characterized in yeast and mammals, our knowledge of a plant ERAD process is rather limited. Here, we report a functional study of an Arabidopsis homolog （AtOS9） of an ER luminal lectin Yos9 （OS-9 in mammals） that recognizes a unique asparagine-linked glycan on misfolded proteins. We discovered that AtOS9 is an ER-Iocalized glyco- protein that is co-expressed with many known/predicted ER chaperones. AT-DNA insertional atos9-t mutation blocks the degradation of a structurally imperfect yet biochemically competent brassinosteroid （BR） receptor bril-9, causing its increased accumulation in the ER and its consequent leakage to the cell surface responsible for restoring the BR sensitivity and suppressing the dwarfism of the bril-9 mutant. In addition, we identified a missense mutation in AtOS9 in a recently discovered ERAD mutant ems-rnutagenized bril suppressor 6 （ebs6-1）. Moreover, we showed that atos9-t also inhibits the ERAD of bril-5, another ER-retained BR receptor, and a misfolded EFR, a BRIl-like receptor for the bacterial translation elongation factor EF-Tu. Furthermore, we found that AtOS9 interacted biochemically and genetically with EBS5, an Arabidopsis homolog of the yeast Hrd3/mammalian SellL known to collaborate with Yos9/OS-9 to select ERAD clients. Taken together, our results demonstrated a functional role of AtOS9 in a plant ERAD process that degrades misfolded receptor-like kinases.
