The lck tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
| Autor: | Kurt E. Amrein, John K. Rose, Bartholomew M. Sefton, David F. Stern, Andrey S. Shaw, Craig Hammond |
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| Rok vydání: | 1989 |
| Předmět: |
Cytoplasm
Macromolecular Substances T-Lymphocytes Molecular Sequence Data Plasma protein binding Biology SH2 domain Transfection General Biochemistry Genetics and Molecular Biology Receptor tyrosine kinase SH3 domain Humans Amino Acid Sequence Tyrosine chemistry.chemical_classification Membrane Glycoproteins Base Sequence Protein-Tyrosine Kinases Phosphoproteins Transmembrane protein chemistry Biochemistry Lymphocyte Specific Protein Tyrosine Kinase p56(lck) CD4 Antigens Mutation biology.protein Protein Multimerization Glycoprotein Oligonucleotide Probes Tyrosine kinase HeLa Cells Plasmids Protein Binding |
| Zdroj: | Cell. 59(4) |
| ISSN: | 0092-8674 |
| Popis: | The CD4 lymphocyte surface glycoprotein and the lck tyrosine protein kinase p56lck are found as a complex in T lymphocytes. We have defined the domains in both proteins that are responsible for this interaction by coexpressing hybrid and deleted forms of the two proteins in HeLa cells. We have found that the unique 32 amino-terminal residues of p56lck and the 38 carboxy-terminal residues of CD4 that comprise the cytoplasmic domain are both necessary and sufficient by themselves for the interaction of the two proteins. The interaction appears to be independent of other T cell-specific proteins and probably occurs before CD4 reaches the cell surface. Our findings suggest that the specialized amino-terminal domains of other members of the src family of intracellular tyrosine kinases may also mediate transmembrane signaling via coupling to the cytoplasmic domains of specific transmembrane proteins. |
| Databáze: | OpenAIRE |
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