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• W2038133088 endingPage "59" @default.
• W2038133088 startingPage "52" @default.
• W2038133088 abstract "CD5 functions as a negative regulator of TCR signaling during thymocyte development, however, the molecular mechanisms involved in this process remain elusive. A key molecule involved in the down modulation of TCR signaling is c-Cbl, an ubiquitin ligase that physically associates with CD5. Crosslinking of TCR in thymocytes leads to ubiquitylation and lysosomal/proteasomal degradation of TCR downstream signaling effectors and CD5 itself. The present report shows that co-engagement of CD3 with CD5 enhanced c-Cbl phosphorylation, which was not affected by the deletion of the pseudo-ITAM domain of CD5, the putative binding site for c-Cbl. However, amino acids present in the carboxy-terminal region of CD5, were necessary for this effect, indicating that ITAM-independent sites were involved in the interaction of c-Cbl with CD5. The carboxy-terminal region of CD5 was also required for Vav degradation, a well-known target for c-Cbl-dependent ubiquitylation. These results support the notion that the distal cytoplasmic domain of CD5, including Y463, plays a relevant role in the downmodulation of TCR signals in thymocytes via c-Cbl." @default.
• W2038133088 created "2016-06-24" @default.
• W2038133088 creator A5011892724 @default.
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• W2038133088 date "2013-03-01" @default.
• W2038133088 modified "2023-10-03" @default.
• W2038133088 title "The carboxy-terminal region of CD5 is required for c-CBL mediated TCR signaling downmodulation in thymocytes" @default.
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• W2038133088 doi "https://doi.org/10.1016/j.bbrc.2013.01.086" @default.
• W2038133088 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23376399" @default.
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