Journal
FEBS LETTERS
Volume 562, Issue 1-3, Pages 160-164Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(04)00223-6
Keywords
glucose-6-phosphatase; diabetes mellitus; membrane topography; endoplasmic reticuluin; proteasome; transmembrane domain
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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.
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