Title : Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation.

Pub. Date : 1997 Jan 1

PMID : 8978305






7 Functional Relationships(s)
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1 We have mapped the site of interaction of CRKL and BCR-ABL to the amino terminal SH3 domain of CRKL with a proline rich region in the C-terminus of ABL. Proline ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens
2 We have mapped the site of interaction of CRKL and BCR-ABL to the amino terminal SH3 domain of CRKL with a proline rich region in the C-terminus of ABL. Proline ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens
3 The proline-rich region was mutated and the effect of this deletion on BCR-ABL transforming function was assayed. Proline ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens
4 In cells expressing the proline deletion mutation of BCR-ABL, CRKL is still tyrosine phosphorylated and forms a complex with BCR-ABL as demonstrated by coimmunoprecipitation. Proline ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens
5 In cells expressing the proline deletion mutation of BCR-ABL, CRKL is still tyrosine phosphorylated and forms a complex with BCR-ABL as demonstrated by coimmunoprecipitation. Proline ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens
6 Our data suggest that the interaction between CRKL and the proline deletion mutant of BCR-ABL is an indirect interaction as CRKL does not interact directly with the proline deletion mutant of BCR-ABL in a gel overlay assay or in a yeast two-hybrid assay. Proline ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens
7 Our data suggest that the interaction between CRKL and the proline deletion mutant of BCR-ABL is an indirect interaction as CRKL does not interact directly with the proline deletion mutant of BCR-ABL in a gel overlay assay or in a yeast two-hybrid assay. Proline ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens