Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly - PubMed (original) (raw)

Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly

J S Bonifacino et al. J Cell Biol. 1989 Jul.

Abstract

The T cell antigen receptor (TCR) is a multisubunit complex composed of at least seven transmembrane chains. The predominant species in most T cells has the composition alpha beta gamma delta epsilon zeta 2. The roles of subunit assembly in transport out of the ER and in the recently described process of pre-Golgi degradation of newly synthesized TCR chains were analyzed in a T-cell line deficient in the synthesis of delta chains (delta 2) and in COS-1 fibroblasts transfected with genes encoding individual TCR chains. Studies with the delta-deficient T-cell line showed that, in the absence of delta, the other TCR chains were synthesized at normal rates, but, instead of being transported to the cell surface, they were retained in the ER. Analysis of the fate of TCR chains retained in the ER showed that they were degraded at vastly different rates by a nonlysosomal pathway. Whereas the alpha chains were degraded rapidly, gamma, zeta, and epsilon were relatively long-lived. To analyze whether this selective degradation was because of different intrinsic susceptibility of the individual chains to degradation or to the formation of resistant oligomers, TCR chains were expressed alone or in combinations in COS-1 fibroblasts. These studies showed that (a) individual TCR chains were degraded at different rates when expressed alone in COS-1 cells, and (b) sensitive chains could be stabilized by coexpression with a resistant chain. Taken together, these observations indicate that both intrinsic sensitivity and subunit assembly play a role in determining the rates at which newly synthesized TCR chains are degraded in the ER.

PubMed Disclaimer

Cited by

Characterization of two human lymphoid cell lines producing human T-lymphotropic virus type I (HTLV-I) isolated from patients with HTLV-I-associated myelopathy or encephalopathy.
Iwata J, Oka T, Furihata M, Sonobe H, Matsubayashi K, Uemura Y, Miyoshi I, Ohtsuki Y. Iwata J, et al. Arch Virol. 1991;118(1-2):101-12. doi: 10.1007/BF01311306. Arch Virol. 1991. PMID: 1675560
Specificity in intracellular protein aggregation and inclusion body formation.
Rajan RS, Illing ME, Bence NF, Kopito RR. Rajan RS, et al. Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13060-5. doi: 10.1073/pnas.181479798. Epub 2001 Oct 30. Proc Natl Acad Sci U S A. 2001. PMID: 11687604 Free PMC article.
The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum.
Yamamoto K, Fujii R, Toyofuku Y, Saito T, Koseki H, Hsu VW, Aoe T. Yamamoto K, et al. EMBO J. 2001 Jun 15;20(12):3082-91. doi: 10.1093/emboj/20.12.3082. EMBO J. 2001. PMID: 11406585 Free PMC article.
Ubiquitination of substrates by esterification.
Wang X, Herr RA, Hansen TH. Wang X, et al. Traffic. 2012 Jan;13(1):19-24. doi: 10.1111/j.1600-0854.2011.01269.x. Epub 2011 Sep 13. Traffic. 2012. PMID: 21883762 Free PMC article. Review.
The transmembrane anchor of the T-cell antigen receptor beta chain contains a structural determinant of pre-Golgi proteolysis.
Wileman T, Carson GR, Shih FF, Concino MF, Terhorst C. Wileman T, et al. Cell Regul. 1990 Nov;1(12):907-19. doi: 10.1091/mbc.1.12.907. Cell Regul. 1990. PMID: 2151609 Free PMC article.

References

1. Mol Cell Biol. 1982 Sep;2(9):1044-51 - PubMed
1. J Cell Biol. 1982 Jan;92(1):92-107 - PubMed
1. J Immunol. 1983 Dec;131(6):2645-50 - PubMed
1. Nucleic Acids Res. 1983 Nov 11;11(21):7631-48 - PubMed
1. Proc Natl Acad Sci U S A. 1983 Nov;80(22):6972-6 - PubMed

MeSH terms

Substances

LinkOut - more resources

Full Text Sources
Other Literature Sources
- The Lens - Patent Citations Database

Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly - PubMed (original) (raw)