Journal
BLOOD
Volume 110, Issue 8, Pages 2974-2982Publisher
AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2007-01-065276
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Funding
- NCI NIH HHS [P30 CA014599, P30 CA 14599-28] Funding Source: Medline
- NIAID NIH HHS [R01 AI044932, R01 AI44932] Funding Source: Medline
- NIGMS NIH HHS [S06 GM008043, S06 GM08043] Funding Source: Medline
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The mucin-like protein CD43 is excluded from the immune synapse, and regulates T-cell proliferation as well as T-cell migration. While the CD43 cytoplasmic domain is necessary for regulation of T-cell activation and proliferation, the mechanism via which CD43 regulates trafficking is not well defined. To investigate whether CD43 phosphorylation regulates its function in T cells, we used tandem mass spectrometry and identified Ser76 in murine CD43 as a previously unidentified site of basal phosphorylation. Interestingly, mutation of this single serine to alanine greatly diminishes T-cell trafficking to the lymph node, while CD43 exclusion and CD43-mediated regulation of T-cell proliferation remain intact. Furthermore, the CD43 extracellular domain was also required for T-cell trafficking, providing a hitherto unknown function for the extracellular domain, and suggesting that the extracellular domain may be required to transduce signals via the cytoplasmic domain. These data reveal a novel mechanism by which CD43 regulates T-cell function, and suggest that CD43 functions as a signaling molecule, sensing extracellular cues and transducing intracellular signals that modulate T-cell function.
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