Abstract:
:The 120-kDa protein product of the c-Cbl proto-oncogene is a ubiquitously expressed cytoplasmic protein that is especially abundant in the thymus, indicating an important role for Cbl in thymic signalling. c-Cbl possesses a highly conserved N-terminal phosphotyrosine binding domain, a C3HC4 RING finger motif, multiple proline-rich motifs, and a number of potential tyrosine phosphorylation sites. Cbl is an early and prominent substrate of protein tyrosine kinases following stimulation of a variety of cell surface receptors, and forms constitutive and inducible associations with a wide range of signalling intermediates. Genetic studies of the Cbl homologue Sli-1 in Caenorhabitis elegans predicted a role for Cbl as a negative regulator of protein tyrosine kinase-mediated signalling pathways. Numerous studies have now shown that expression of Cbl and its oncogenic variants can indeed modulate signalling from activated protein tyrosine kinases. The present review highlights some of the recent developments in our understanding of Cbl function, with particular reference to its participation and possible roles in TCR-mediated signalling.
journal_name
Immunol Cell Bioljournal_title
Immunology and cell biologyauthors
Thien CB,Langdon WYdoi
10.1046/j.1440-1711.1998.00768.xsubject
Has Abstractpub_date
1998-10-01 00:00:00pages
473-82issue
5eissn
0818-9641issn
1440-1711pii
768journal_volume
76pub_type
杂志文章,评审abstract::There are estimated to be 350 million chronic carriers of hepatitis B infection worldwide. Patients with chronic hepatitis B are at risk of liver cirrhosis with associated mortality because of hepatocellular carcinoma and other complications. An important goal, therefore, is the development of an effective therapeutic...
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journal_title:Immunology and cell biology
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journal_title:Immunology and cell biology
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