Negative regulation of Lck by Cbl ubiquitin ligase.

The Cbl-family ubiquitin ligases function as negative regulators of activated receptor tyrosine kinases by facilitating their ubiquitination and subsequent targeting to lysosomes. Cbl associates with the lymphoid-restricted nonreceptor tyrosine kinase Lck, but the functional relevance of this interaction remains unknown. Here, we demonstrate that T cell receptor and CD4 coligation ...
on human T cells results in enhanced association between Cbl and Lck, together with Lck ubiquitination and degradation. A Cbl(-/-) T cell line showed a marked deficiency in Lck ubiquitination and increased levels of kinase-active Lck. Coexpression in 293T cells demonstrated that Lck kinase activity and Cbl ubiquitin ligase activity were essential for Lck ubiquitination and negative regulation of Lck-dependent serum response element-luciferase reporter activity. The Lck SH3 domain was pivotal for Cbl-Lck association and Cbl-mediated Lck degradation, with a smaller role for interactions mediated by the Cbl tyrosine kinase-binding domain. Finally, analysis of a ZAP-70-deficient T cell line revealed that Cbl inhibited Lck-dependent mitogen-activated protein kinase activation, and an intact Cbl RING finger domain was required for this functional effect. Our results demonstrate a direct, ubiquitination-dependent, negative regulatory role of Cbl for Lck in T cells, independent of Cbl-mediated regulation of ZAP-70.
Mesh Terms:
Antigens, CD4, Cell Line, Enzyme Activation, Gene Deletion, Genes, Reporter, Humans, Jurkat Cells, Ligases, Lymphocyte Activation, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Protein Binding, Protein Processing, Post-Translational, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Receptors, Antigen, T-Cell, T-Lymphocytes, Ubiquitin, Ubiquitin-Protein Ligases, ZAP-70 Protein-Tyrosine Kinase, src Homology Domains
Proc. Natl. Acad. Sci. U.S.A.
Date: Mar. 19, 2002
Download Curated Data For This Publication
4995
Switch View:
  • Interactions 1