Novel Aspects of Degradation of T Cell Receptor Subunits from the Endoplasmic Reticulum (ER) in T Cells: Importance of Oligosaccharide Processing, Ubiquitination, and Proteasome-dependent Removal from ER Membranes

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J. Exp. Med., Volume 187, Number 6, March 16, 1998 835-846

Novel Aspects of Degradation of T Cell Receptor Subunits from the Endoplasmic Reticulum (ER) in T Cells: Importance of Oligosaccharide Processing, Ubiquitination, and Proteasome-dependent Removal from ER Membranes

By Mei Yang,^* Satoshi mura, Juan S. Bonifacino,^§ and Allan M. Weissman^*

From the ^* Laboratory of Immune Cell Biology, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-1152; The Kitasato Institute, Tokyo, Japan; and the ^§ Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-5430

Expression of the T cell antigen receptor (TCR) on the surface of thymocytes and mature T cells is dependent on the assemblyof receptor subunits into TCRs in the endoplasmic reticulum (ER)and their successful traversal of the secretory pathway to theplasma membrane. TCR subunits that fail to exit the ER for theGolgi complex are degraded by nonlysosomal processes that havebeen referred to as "ER degradation". The molecular basis forthe loss of the TCR CD3- $delta$ and TCR- $alpha$ subunits from the ER was investigatedin lymphocytes. For CD3- $delta$ , we describe a process leading to itsdegradation that includes trimming of mannose residues from asparagine-linked(N-linked) oligosaccharides, generation of ubiquitinated membrane-boundintermediates, and proteasome-dependent removal from the ER membrane.When either mannosidase activity or the catalytic activity ofproteasomes was inhibited, loss of CD3- $delta$ was markedly curtailedand CD3- $delta$ remained membrane bound in a complex with CD3- $epsilon$ . TCR- $alpha$ was also found to be degraded in a proteasome-dependent mannerwith ubiquitinated intermediates. However, no evidence of a rolefor mannosidases was found for TCR- $alpha$ , and significant retrogrademovement through the ER membrane took place even when proteasomefunction was inhibited. These findings provide new insights intomechanisms employed to regulate levels of TCRs, and underscorethat cells use multiple mechanisms to target proteins from theER to the cytosol for degradation.

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