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Human CD6 possesses a large, alternatively spliced cytoplasmic domain
W H Robinson1, H E Neuman de Vegvar, S S Prohaska
1Department of Medicine, Stanford University School of Medicine, CA 94305-5487, USA.
European Journal of Immunology
|October 1, 1995
Summary
Researchers discovered a previously unrecognized, large cytoplasmic domain in human CD6, crucial for T cell activation. This finding clarifies CD6 signaling pathways and T cell proliferation responses.
Area of Science:
- Immunology
- Molecular Biology
- Cell Biology
Background:
- Human CD6 is a T cell surface glycoprotein involved in T cell activation.
- A size discrepancy existed between human (44 amino acids) and mouse (243 amino acids) CD6 cytoplasmic domains.
Purpose of the Study:
- To isolate and characterize the full-length human CD6 cytoplasmic domain.
- To investigate the functional implications of the human CD6 cytoplasmic domain in T cell signaling.
Main Methods:
- Reverse transcriptase-polymerase chain reaction (RT-PCR) of human peripheral blood lymphocyte mRNA.
- Nucleotide sequencing of human CD6 cDNA clones.
- Immunoprecipitation and SDS-PAGE analysis of transfected cells.
Main Results:
- A novel human CD6 cDNA clone (CD6-PB1) predicts a 244-amino acid cytoplasmic domain, similar in size to mouse CD6.
- This domain contains motifs for SH3 binding, protein kinase C, and casein kinase-2 phosphorylation.
- Alternative splicing variants of human CD6 were identified.
Conclusions:
- Human CD6 possesses a large, previously unrecognized cytoplasmic domain critical for T cell activation.
- This domain contains signaling motifs likely involved in T cell proliferation upon CD6 ligation.
- Correct characterization of human CD6 is essential for understanding T cell signaling pathways.