Cytoplasmic tail deletion of T cell receptor (TCR) beta-chain results in its surface expression as glycosylphosphatidylinositol-anchored polypeptide on mature T cells in the absence of TCR-alpha.

Bell, L. M.; Solomon, Keith R.; Gold, Jeffrey P.; Tan, Kut-Nie

doi:10.1016/s0021-9258(17)31710-6

Cited by 13 publications

(1 citation statement)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We, however, found that some proteins would get expressed as a GPI-anchored protein if the cytoplasmic region were removed, as the transmembrane region serves as a GPI-anchoring signal sequence. There are other examples in the literature where such a phenomenon has been reported (Mitchell et al, 1991;Bell et al, 1994;Jacobs et al, 1996). Fortunately, the characteristics of a GPI-anchoring signal sequence are well understood, and there exist bioinformatics programs that can predict with confidence whether a protein would become GPI-anchored when expressed (Eisenhaber et al, 1998;Eisenhaber et al, 1999).…”

Section: Design Construction and Purification Of Tailless Transmembra...mentioning

confidence: 99%

Supported Lipid Bilayer Technology for the Study of Cellular Interfaces

et al. 2015

View full text Add to dashboard Cite

Glass‐supported lipid bilayers presenting freely diffusing proteins have served as a powerful tool for studying cell‐cell interfaces, in particular, T cell–antigen presenting cell (APC) interactions, using optical microscopy. Here we expand upon existing protocols and describe the preparation of liposomes by an extrusion method, and describe how this system can be used to study immune synapse formation by Jurkat cells. We also present a method for forming such lipid bilayers on silica beads for the study of signaling responses by population methods, such as western blotting, flow cytometry, and gene‐expression analysis. Finally, we describe how to design and prepare transmembrane‐anchored protein‐laden liposomes, following expression in suspension CHO (CHOs) cells, a mammalian expression system alternative to insect and bacterial cell lines, which do not produce mammalian glycosylation patterns. Such transmembrane‐anchored proteins may have many novel applications in cell biology and immunology. © 2015 by John Wiley & Sons, Inc.

show abstract

Section: Design Construction and Purification Of Tailless Transmembra...mentioning

confidence: 99%

Supported Lipid Bilayer Technology for the Study of Cellular Interfaces

et al. 2015

View full text Add to dashboard Cite

show abstract

T cell receptor α‐chain tail is required for protein kinase C‐mediated down‐regulation, but not for signaling

Bt¹,

Rubin

Peter³

et al. 1997

Eur J Immunol

View full text Add to dashboard Cite

Antigen stimulation through the T cell receptor (TCR) induces phosphorylation of the associated CD3 gamma delta epsilon- and zeta-chain cytoplasmic tails. These events lead to the induction of the intracellular signaling pathways with concomitant receptor down-regulation. The TCR is down-regulated from the cell surface by the activation of protein kinase, C (PKC) and subsequent serine phosphorylation of the CD3 gamma-chain. We report here that the TCR alpha-chain cytoplasmic tail is also necessary for PKC-mediated internalization of the TCR complex. The requirement for the TCR alpha-chain cytoplasmic tail is specific for internalization of the TCR complex, since down-regulation of CD4 is still intact in hybridoma cells expressing a tailless TCR alpha-chain. The absence of TCR internalization directly correlates with defective PKC-mediated phosphorylation of the CD3 gamma-chain. Despite deficient PKC-mediated TCR down-regulation, the tailless alpha beta TCR still transduces antigenic signals resulting in the production of interleukin-2. Although the TCR tails are not obviously required for signal transduction, the TCR alpha-tail may serve as a targeting domain for PKC-mediated down-regulation of the TCR complex.

show abstract

The Interchain Disulfide Linkage of T-Cell Antigen Receptor-α and -β Chains Is a Prerequisite for T-Cell Activation

Kemp

et al. 1998

Cellular Immunology

View full text Add to dashboard Cite

Cytoplasmic tail deletion of T cell receptor (TCR) beta-chain results in its surface expression as glycosylphosphatidylinositol-anchored polypeptide on mature T cells in the absence of TCR-alpha.

Cited by 13 publications

References 47 publications

Supported Lipid Bilayer Technology for the Study of Cellular Interfaces

Supported Lipid Bilayer Technology for the Study of Cellular Interfaces

T cell receptor α‐chain tail is required for protein kinase C‐mediated down‐regulation, but not for signaling

The Interchain Disulfide Linkage of T-Cell Antigen Receptor-α and -β Chains Is a Prerequisite for T-Cell Activation

Contact Info

Product

Resources

About