DOI: 10.4049/jimmunol.165.4.2068. Essential Role of CD8 Palmitoylation in CD8 Coreceptor Function

Essential Role of CD8 Palmitoylation in CD8 Coreceptor Function

10.4049/jimmunol.165.4.2068

Crossref journal-article

Oxford University Press (OUP)

The Journal of Immunology (286)

Abstract

Abstract To investigate the molecular basis that makes heterodimeric CD8αβ a more efficient coreceptor than homodimeric CD8αα, we used various CD8 transfectants of T1.4 T cell hybridomas, which are specific for H-2Kd, and a photoreactive derivative of the Plasmodium berghei circumsporozoite peptide PbCS 252–260 (SYIPSAEKI). We demonstrate that CD8 is palmitoylated at the cytoplasmic tail of CD8β and that this allows partitioning of CD8αβ, but not of CD8αα, in lipid rafts. Localization of CD8 in rafts is crucial for its coreceptor function. First, association of CD8 with the src kinase p56lck takes place nearly exclusively in rafts, mainly due to increased concentration of both components in this compartment. Deletion of the cytoplasmic domain of CD8β abrogated localization of CD8 in rafts and association with p56lck. Second, CD8-mediated cross-linking of p56lck by multimeric Kd-peptide complexes or by anti-CD8 Ab results in p56lck activation in rafts, from which the abundant phosphatase CD45 is excluded. Third, CD8-associated activated p56lck phosphorylates CD3ζ in rafts and hence induces TCR signaling and T cell activation. This study shows that palmitoylation of CD8β is required for efficient CD8 coreceptor function, mainly because it dramatically increases CD8 association with p56lck and CD8-mediated activation of p56lck in lipid rafts.

Bibliography

Arcaro, A., GreÌgoire, C., Boucheron, N., Stotz, S., Palmer, E., Malissen, B., & Luescher, I. F. (2000). Essential Role of CD8 Palmitoylation in CD8 Coreceptor Function. The Journal of Immunology, 165(4), 2068â2076.

Authors 7

Alexandre Arcaro (first)
Claude Grégoire (additional)
Nicole Boucheron (additional)
Sabine Stotz (additional)
Ed Palmer (additional)
Bernard Malissen (additional)
Immanuel F. Luescher (additional)

References 47 Referenced 138

Dates

Type	When
Created	11 years, 4 months ago (April 20, 2014, 8:29 p.m.)
Deposited	7 months, 4 weeks ago (Jan. 2, 2025, 11:54 a.m.)
Indexed	3 weeks, 6 days ago (Aug. 5, 2025, 8:35 a.m.)
Issued	25 years ago (Aug. 15, 2000)
Published	25 years ago (Aug. 15, 2000)
Published Print	25 years ago (Aug. 15, 2000)

Funders 0

None

BibTeX

@article{Arcaro_2000, title={Essential Role of CD8 Palmitoylation in CD8 Coreceptor Function}, volume={165}, ISSN={1550-6606}, url={http://dx.doi.org/10.4049/jimmunol.165.4.2068}, DOI={10.4049/jimmunol.165.4.2068}, number={4}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Arcaro, Alexandre and Grégoire, Claude and Boucheron, Nicole and Stotz, Sabine and Palmer, Ed and Malissen, Bernard and Luescher, Immanuel F.}, year={2000}, month=aug, pages={2068–2076} }

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  "abstract": "<jats:title>Abstract</jats:title>\n               <jats:p>To investigate the molecular basis that makes heterodimeric CD8\u03b1\u03b2 a more efficient coreceptor than homodimeric CD8\u03b1\u03b1, we used various CD8 transfectants of T1.4 T cell hybridomas, which are specific for H-2Kd, and a photoreactive derivative of the Plasmodium\u2008berghei circumsporozoite peptide PbCS 252\u2013260 (SYIPSAEKI). We demonstrate that CD8 is palmitoylated at the cytoplasmic tail of CD8\u03b2 and that this allows partitioning of CD8\u03b1\u03b2, but not of CD8\u03b1\u03b1, in lipid rafts. Localization of CD8 in rafts is crucial for its coreceptor function. First, association of CD8 with the src kinase p56lck takes place nearly exclusively in rafts, mainly due to increased concentration of both components in this compartment. Deletion of the cytoplasmic domain of CD8\u03b2 abrogated localization of CD8 in rafts and association with p56lck. Second, CD8-mediated cross-linking of p56lck by multimeric Kd-peptide complexes or by anti-CD8 Ab results in p56lck activation in rafts, from which the abundant phosphatase CD45 is excluded. Third, CD8-associated activated p56lck phosphorylates CD3\u03b6 in rafts and hence induces TCR signaling and T cell activation. This study shows that palmitoylation of CD8\u03b2 is required for efficient CD8 coreceptor function, mainly because it dramatically increases CD8 association with p56lck and CD8-mediated activation of p56lck in lipid rafts.</jats:p>",
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