期刊论文详细信息
FEBS Letters
Direct interaction of nerve growth factor receptor, TrkA, with non‐receptor tyrosine kinase, c‐Abl, through the activation loop
Koch, Alexandra1  Mancini, Annalisa1  Stefan, Monica1  Niemann, Heiner1  Niedenthal, Rainer1  Tamura, Teruko1 
[1] Institut für Biochemie, OE 4310, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, 30623 Hannover, Germany
关键词: TrkA-interacting protein;    c-Abl tyrosine kinase;    SH2-B;    Kinase activation loop;   
DOI  :  10.1016/S0014-5793(00)01242-4
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

The nerve growth factor receptor, TrkA, is essential for the survival and differentiation of neurons in the central and peripheral nervous systems. To understand the molecular principles underlying this differentiation step, we employed a yeast two-hybrid screening protocol using human TrkA as bait. We isolated c-Abl as a TrkA-interacting protein, in addition to known proteins such as phospholipase Cγ and SH2-B. This interaction was confirmed by an in vitro binding assay using glutathione S-tranferase–Abl fusion protein. Furthermore, we show here that c-Abl binds to phosphotyrosine residue(s) in the kinase activation loop of TrkA.

【 授权许可】

Unknown   

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