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Direct interaction of nerve growth factor receptor, TrkA, with non‐receptor tyrosine kinase, c‐Abl, through the activation loop
Author(s) -
Koch Alexandra,
Mancini Annalisa,
Stefan Monica,
Niedenthal Rainer,
Niemann Heiner,
Tamura Teruko
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01242-4
Subject(s) - tropomyosin receptor kinase a , ror1 , tropomyosin receptor kinase c , receptor tyrosine kinase , low affinity nerve growth factor receptor , tyrosine kinase , proto oncogene tyrosine protein kinase src , chemistry , cancer research , nerve growth factor , microbiology and biotechnology , tropomyosin receptor kinase b , platelet derived growth factor receptor , receptor , biology , biochemistry , growth factor , neurotrophic factors
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.