TGN38/41的过表达导致γ-衔接蛋白定位错误。
Overexpression of TGN38/41 leads to mislocalisation of gamma-adaptin.
作者信息
Reaves B, Banting G
机构信息
Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, UK.
出版信息
FEBS Lett. 1994 Sep 12;351(3):448-56. doi: 10.1016/0014-5793(94)00813-2.
Abstract
TGN38 and TGN41 are isoforms of a monotopic integral membrane protein which recycles between the trans Golgi network (TGN) and the cell surface, but which, at steady state, is predominantly located in the TGN. Full-length and truncated versions of rat TGN38/41 have been expressed in monkey (COS) and human (Heb7a) cells under the control of the heavy metal inducible Metallothionein IIA promoter. This has allowed the regulated expression of TGN38/41 protein constructs to different levels in the transfected cells. These studies show that (i) controlled overexpression of TGN38/41 results in mislocalisation to parts of the endocytic pathway, (ii) a truncated version of TGN38/41, lacking the cytoplasmic domain, remains in the TGN, and (iii) there is a direct or indirect interaction between the cytoplasmic domain of TGN38/41 and gamma-adaptin.
摘要
TGN38和TGN41是一种单拓扑整合膜蛋白的同工型，该蛋白在反式高尔基体网络（TGN）和细胞表面之间循环，但在稳态时主要位于TGN中。大鼠TGN38/41的全长和截短版本已在重金属诱导型金属硫蛋白IIA启动子的控制下在猴（COS）和人（Heb7a）细胞中表达。这使得TGN38/41蛋白构建体在转染细胞中能够被调控表达至不同水平。这些研究表明：（i）TGN38/41的可控过表达导致其错误定位于内吞途径的部分区域；（ii）缺少胞质结构域的TGN38/41截短版本仍保留在TGN中；（iii）TGN38/41的胞质结构域与γ-衔接蛋白之间存在直接或间接的相互作用。
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