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Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor

✍ Scribed by Hiroko Yano; Feng Cong; Raymond B. Birge; Stephen P. Goff; Moses V. Chao

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
146 KB
Volume
59
Category
Article
ISSN
0360-4012

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✦ Synopsis

Nerve growth factor (NGF) initiates the majority of its biological effects by promoting the dimerization and activation of the tyrosine kinase receptor TrkA. In addition to rapid increases in the phosphorylation of phosphatidylinositol 3Јkinase (PI 3-kinase) and phospholipase C-␥ and increased ras activity, phosphorylation of c-Crk and paxillin proteins has been observed upon TrkA activation. The c-Abl tyrosine kinase is involved in the control of the axonal cytoskeleton and is known to interact with c-Crk proteins.

Here we have tested the possibility that TrkA receptors might form an association with the c-Abl protein. After transfection in 293T cells, TrkA and c-Abl kinases could be coimmunoprecipitated. This interaction did not require TrkA receptors to be autophosphorylated. Mapping analysis indicated that the region of c-Abl association was confined to the juxtamembrane region of TrkA. The interaction of c-Abl with TrkA was also observed in differentiated pheochromocytoma PC12 cells. These results suggest that c-Abl may be recruited to the NGF receptor complex and be involved in regulating specific phosphorylation events that occur during neuronal differentiation.

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