Nilsson T, Jackson M, Peterson P A
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Cell. 1989 Aug 25;58(4):707-18. doi: 10.1016/0092-8674(89)90105-0.
The adenoviral transmembrane E3/19K glycoprotein is a resident of the endoplasmic reticulum. Here we show that the last six amino acid residues of the 15-membered cytoplasmic tail are necessary and sufficient for the ER retention. These residues can be transplanted onto the cytoplasmic tail of other membrane-bound proteins such that ER residency is conferred. Deletion analysis demonstrated that no single amino acid residue is responsible for the retention. The identified structural motif must occupy the extreme COOH-terminal position to be functional. An endogenous transmembrane ER protein, UDP-glucuronosyltransferase, also contains a retention signal in its cytoplasmic tail. We suggest that short linear sequences occupying the extreme COOH-terminal position of transmembrane ER proteins serve as retention signals.
腺病毒跨膜E3/19K糖蛋白是内质网的驻留蛋白。我们在此表明，15个氨基酸的细胞质尾的最后六个氨基酸残基对于内质网保留是必需且充分的。这些残基可以移植到其他膜结合蛋白的细胞质尾上，从而赋予内质网驻留特性。缺失分析表明，没有单个氨基酸残基负责保留。所鉴定的结构基序必须占据极端的COOH末端位置才能发挥功能。一种内源性跨膜内质网蛋白，UDP-葡萄糖醛酸基转移酶，在其细胞质尾中也含有一个保留信号。我们认为，占据跨膜内质网蛋白极端COOH末端位置的短线性序列作为保留信号。
