Mori K, Ma W, Gething M J, Sambrook J
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.
Cell. 1993 Aug 27;74(4):743-56. doi: 10.1016/0092-8674(93)90521-q.
In eukaryotic cells, the accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers a signaling pathway from the ER to the nucleus. Several yeast mutants defective in this pathway map to the ERN1 gene, which protects cells from lethal consequences of stress by signaling for increased expression of BiP and other ER proteins. ERN1 encodes a 1115 amino acid transmembrane protein (Ern1p) whose glycosylated N-terminal portion is located inside microsomes and whose cytoplasmic C-terminal portion carries an essential protein kinase activity. We postulate that Ern1p is the proximal sensor of events in the ER and that binding of ligand causes transduction of information across the ER membrane, leading to activation of a specific set of transcription factors.
在真核细胞中，内质网（ER）中未折叠蛋白的积累触发了一条从内质网到细胞核的信号通路。该信号通路中存在缺陷的几个酵母突变体被定位到ERN1基因，该基因通过发出信号增加BiP和其他内质网蛋白的表达，保护细胞免受应激的致命影响。ERN1编码一种1115个氨基酸的跨膜蛋白（Ern1p），其糖基化的N端部分位于微粒体内，其胞质C端部分具有必需的蛋白激酶活性。我们推测Ern1p是内质网中事件的近端传感器，配体的结合导致信息跨内质网膜转导，从而激活一组特定的转录因子。
