SUBSTRATE PHOSPHORYLATION SPECIFICITY OF THE HUMAN C-KIT RECEPTOR TYROSINE KINASE

被引:0
作者
HERBST, R
LAMMERS, R
SCHLESSINGER, J
ULLRICH, A
机构
[1] MAX PLANCK INST BIOCHEM,DEPT MOLEC BIOL,KLOPFERSPITZ 18A,W-8033 MARTINSRIED,GERMANY
[2] NYU MED CTR,DEPT PHARMACOL,NEW YORK,NY 10016
关键词
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The chimeric EK-receptor (EK-R), consisting of the epidermal growth factor receptor (EGF-R) extracellular binding domain and p145c-kit cytoplasmic signal-generating sequences, was fully functional in forming high and low affinity EGF binding sites and in ligand-regulated receptor and substrate phosphorylation activities. Relative to EGF-R, EK-R activation stimulated kit-characteristic phosphorylation of human 293 fibroblast substrate polypeptides. Transient coexpression of EK-R with candidate substrates resulted in ligand-induced phosphorylation of phospholipase C-gamma and guanosine trisphosphatase-activating polypeptide. The RAF-1 serine/threonine kinase was shown to be associated with activated EK-R, but no tyrosine phosphorylation could be detected. The faithfulness of EK-R substrate phosphorylation specificity was confirmed with stem cell factor-stimulated p145c-kit.
引用
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页码:19908 / 19916
页数:9
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