The lysine residue in the membrane-spanning domain of the beta chain is necessary for cell surface expression of the T cell antigen receptor

doi:10.1084/jem.168.6.1971

This Article

	Full Text (PDF)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JEM
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Morley, B. J.
	Articles by Weiss, A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Morley, B. J.
	Articles by Weiss, A.


Social Bookmarking

	What's this?

ARTICLES

The lysine residue in the membrane-spanning domain of the beta chain is necessary for cell surface expression of the T cell antigen receptor

BJ Morley, KN Chin, ME Newton and A Weiss
Howard Hughes Medical Institute, Department of Medicine, University of California, San Francisco 94143.

The TCR is a complex receptor composed of seven polypeptide chains consisting of a ligand-binding subunit, Ti, and a putative signal- transducing subunit, CD3. Phylogenetically conserved charged amino acid residues within the membrane-spanning domains present in all seven chains of the TCR have been proposed to be important in the association between Ti and CD3. Using a Ti beta chain-deficient mutant of the cell line Jurkat, site-directed mutagenesis and transfection of Ti beta chain cDNA was performed to assess the importance of the lysine residue at position 290 within the membrane-spanning domain of the Ti beta chain to expression of the TCR complex. These studies demonstrated that the lysine residue, and not simply conservation of either basic charge or secondary structure, is important at this position.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Arnett, K. L., Harrison, S. C., Wiley, D. C. (2004). Crystal structure of a human CD3-{epsilon}/{delta} dimer in complex with a UCHT1 single-chain antibody fragment. Proc. Natl. Acad. Sci. USA 101: 16268-16273 [Abstract] [Full Text]
Ouellet, M., Barbeau, B., Tremblay, M. J. (1999). p56lck, ZAP-70, SLP-76, and Calcium-regulated Effectors Are Involved in NF-kappa B Activation by Bisperoxovanadium Phosphotyrosyl Phosphatase Inhibitors in Human T Cells. J. Biol. Chem. 274: 35029-35036 [Abstract] [Full Text]
Morton, H. C., van den Herik-Oudijk, I. E., Vossebeld, P., Snijders, A., Verhoeven, A. J., Capel, P. J. A., van de Winkel, J. G. J. (1995). Functional Association between the Human Myeloid Immunoglobulin A Fc Receptor (CD89) and FcR [IMAGE] Chain. J. Biol. Chem. 270: 29781-29787 [Abstract] [Full Text]
Wegener, A.-M. K., Hou, X., Dietrich, J., Geisler, C. (1995). Distinct Domains of the CD3-[IMAGE] Chain Are Involved in Surface Expression and Function of the T Cell Antigen Receptor. J. Biol. Chem. 270: 4675-4680 [Abstract] [Full Text]
Manolios, N, Bonifacino, J., Klausner, R. (1990). Transmembrane helical interactions and the assembly of the T cell receptor complex. Science 249: 274-277 [Abstract]