期刊
FEBS LETTERS
卷 562, 期 1-3, 页码 160-164出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(04)00223-6
关键词
glucose-6-phosphatase; diabetes mellitus; membrane topography; endoplasmic reticuluin; proteasome; transmembrane domain
The islet-specific glucose-6-phosphatase-related protein (IGRP) has no known catalytic activity, but is of interest because it is the source of the peptide autoantigen targeted by a prevalent population of pathogenic CD8(+) T cells in non-obese diabetic mice. To better understand the potential roles of this protein in diabetes mellitus, we examine the subcellular localization and membrane topography of human IGRP. We show that IGRP is a glycoprotein, held in the endoplasmic reticulum by nine transmembrane domains, which is degraded in cells predominantly through the proteasome pathway that generates the major histocompatibility complex class I-presented peptides. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据