The signaling pathways underlying starvation-induced upregulation of α-mannosidase Ams1 in Saccharomyces cerevisiae
The signaling pathways underlying starvation-induced upregulation of α-mannosidase Ams1 in Saccharomyces cerevisiae
复制标题
酿酒酵母饥饿诱导的 α-甘露糖苷酶 Ams1 上调的信号通路
DOI:
10.1016/j.bbagen.2016.02.018
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发表时间:
2016
期刊:
影响因子:
--
通讯作者:
Wakayama M.
中科院分区:
文献类型:
--
作者:
Umekawa M;Ujihara M;Makishima K;Yamamoto S;Takematsu H;Wakayama M.
BackgroundCells have evolved the mechanisms to survive nutritional shortages in the environment. InSaccharomyces cerevisiae, α-mannosidase Ams1 is known to play a role in catabolism ofN-linked free oligosaccharides in the cytosol. Although, this enzyme is also known to be transported selectively from the cytosol to the vacuoles by autophagy, the physiological significance of this transport has not been clarified.MethodsTo elucidate the regulatory mechanism of the activity of Ams1, we assessed the enzymatic activity of the cell free extract of the wild-type and various gene disruptants under different nutritional conditions. In addition, the regulation of Ams1 at both transcription and post-translation was examined.ResultsThe activity of Ams1 was significantly increased upon the depletion of glucose in the medium. Interestingly, the activity of the enzyme was also stimulated by nitrogen starvation. Our data showed that the activity of Ams1 is regulated by the stress responsive transcriptional factors Msn2/4 through the protein kinase A and the target of rapamycin complex 1 pathways. In addition, Ams1 is post-translationally activated by Pep4-dependent processing in the vacuoles.ConclusionYeast cells monitor extracellular nutrients to regulate mannoside catabolismviathe cellular signaling pathway.General significanceThis study revealed that intracellular Ams1 activity is exquisitely upregulated in response to nutrient starvation by induced expression as well as by Pep4-dependent enhanced activity in the vacuoles. The signaling molecules responsible for regulation of Ams1 were also clarified.