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TGN38胞质结构域中的SXYQRL序列在反式高尔基体网络定位中起主要作用。

The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization.

作者信息

Wong S H, Hong W

机构信息

Membrane Biology Laboratory, National University of Singapore.

出版信息

J Biol Chem. 1993 Oct 25;268(30):22853-62.

PMID:8226795
Abstract

The trans-Golgi network (TGN) plays a central role in protein sorting/targeting. TGN38 is an integral membrane protein confined mainly to the TGN. When the cytoplasmic 32-residue sequence of TGN38 was fused to the ecto- and transmembrane domains of glycophorin A (a surface protein), the resulting chimeric protein was localized to the TGN. Detailed mutagenesis of the 32-residue sequence revealed that the Ser, Tyr, and Leu residues at positions 23, 25, and 28, respectively, are essential for TGN localization. Further studies demonstrate that the sequence SXYQRL can by itself confer significant TGN localization.

摘要

反式高尔基体网络(TGN)在蛋白质分选/靶向过程中起着核心作用。TGN38是一种主要局限于TGN的整合膜蛋白。当TGN38的32个氨基酸残基的胞质序列与血型糖蛋白A(一种表面蛋白)的胞外和跨膜结构域融合时,所产生的嵌合蛋白定位于TGN。对这32个氨基酸残基序列进行详细的诱变分析表明,第23、25和28位的丝氨酸、酪氨酸和亮氨酸残基对于TGN定位至关重要。进一步的研究表明,序列SXYQRL自身就能赋予显著的TGN定位能力。

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