IDENTIFICATION OF A CONSENSUS MOTIF FOR RETENTION OF TRANSMEMBRANE PROTEINS IN THE ENDOPLASMIC-RETICULUM
IDENTIFICATION OF A CONSENSUS MOTIF FOR RETENTION OF TRANSMEMBRANE PROTEINS IN THE ENDOPLASMIC-RETICULUM
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DOI：
10.1002/j.1460-2075.1990.tb07513.x
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发表时间：
1990-10-01
期刊：
影响因子：
11.4
通讯作者：
PETERSON, PA
中科院分区：
文献类型：
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作者：
JACKSON, MR;NILSSON, T;PETERSON, PA
跨膜内质网 (ER) 蛋白的几个家族在其暴露于细胞质的尾部含有保留基序。突变分析表明，位于 C 末端三个、四个或五个残基处的两个赖氨酸代表保留基序。在距 Lyt2 末端三个残基的赖氨酸之前引入赖氨酸，使得该细胞表面蛋白成为 ER 的常驻蛋白。同样，多聚丝氨酸序列中两个赖氨酸残基的适当定位将标记蛋白限制在 ER 内。精氨酸或组氨酸不能替代赖氨酸，这表明简单的电荷相互作用不足以解释保留。识别出的共有基序可以作为检索信号，将蛋白质从内质网附近的分选室带回。
Several families of transmembrane endoplasmic reticulum (ER) proteins contain retention motifs in their cytoplasmically exposed tails. Mutational analyses demonstrated that two lysines positioned three and four or five residues from the C-terminus represent the retention motif. The introduction of a lysine preceding the lysine that occurs three residues from the terminus of Lyt2 renders this cell surface protein a resident of the ER. Likewise, the appropriate positioning of two lysine residues in a poly-serine sequence confines marker proteins to the ER. Arginines or histidines cannot replace lysines, suggesting that simple charge interactions are not sufficient to explain the retention. The identified consensus motif may serve as a retrieval signal that brings proteins back from a sorting compartment adjacent to the ER.