Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 26 March 1993:
Vol. 259. no. 5103, pp. 1901 - 1904
DOI: 10.1126/science.8456316
Prev | Table of Contents | Next

Articles

Science, Vol 259, Issue 5103, 1901-1904
Copyright © 1993 by American Association for the Advancement of Science

articles

Translocation of TCR alpha chains into the lumen of the endoplasmic reticulum and their degradation

J Shin, S Lee, and JL Strominger

Division of Tumor Virology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.

After synthesis, the alpha chain of the T cell antigen receptor (TCR alpha) can form a complex with other TCR chains and move to the cell surface, or TCR alpha can undergo degradation in the endoplasmic reticulum (ER) if it remains unassembled. The mechanism of translocation and degradation in the ER is unclear. It was found that the putative transmembrane region of TCR alpha (alpha tm) was incompetent on its own to act as a transmembrane region. Molecules that contained alpha tm were translocated into the ER lumen and then underwent either rapid degradation or secretion, depending on the sequence of the cytoplasmic domain. A specific signal for ER degradation within alpha tm does not appear to be present.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
An Endoplasmic Reticulum Retention Signal Located in the Extracellular Amino-terminal Domain of the NR2A Subunit of N-Methyl-D-aspartate Receptors.
S. Qiu, X.-m. Zhang, J.-y. Cao, W. Yang, Y.-g. Yan, L. Shan, J. Zheng, and J.-h. Luo (2009)
J. Biol. Chem. 284, 20285-20298
   Abstract »    Full Text »    PDF »
Endoplasmic Reticulum-associated Degradation of Mammalian Glycoproteins Involves Sugar Chain Trimming to Man6-5GlcNAc2.
Z. Frenkel, W. Gregory, S. Kornfeld, and G. Z. Lederkremer (2003)
J. Biol. Chem. 278, 34119-34124
   Abstract »    Full Text »    PDF »
Recognition of a Single Transmembrane Degron by Sequential Quality Control Checkpoints.
L. Fayadat and R. R. Kopito (2003)
Mol. Biol. Cell 14, 1268-1278
   Abstract »    Full Text »    PDF »
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.
M. Yang, S. Omura, J. S. Bonifacino, and A. M. Weissman (1998)
J. Exp. Med. 187, 835-846
   Abstract »    Full Text »    PDF »
Reglucosylation of N-Linked Glycans Is Critical for Calnexin Assembly with T Cell Receptor (TCR) alpha Proteins but Not TCRbeta Proteins.
J. E.M. Van Leeuwen and K. P. Kearse (1997)
J. Biol. Chem. 272, 4179-4186
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)