Abstract
Previous work showed that integrin stimulation triggers activation of the c-Abl tyrosine kinase and its transient localization to focal adhesions. We now report that plating cells on fibronectin triggers association of Grb2 with c-Abl, suggesting possible involvement of c-Abl with integrin activation of the MAP kinase pathway. Expression of a kinase-defective c-Abl specifically inhibited the transient induction of Erk2 activity following cell adhesion. Together with the known ability of activated, oncogenic forms of c-Abl to activate Ras and the MAP kinase pathway, these data suggest that c-Abl contributes to the integrin induction of MAP kinase activity.
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Acknowledgements
We thank Jean Wang for providing Abl−/− cells and 8E9 antibody, and Joan Brugge for providing antibody EC10 against chicken Src. We thank Tony Truong for outstanding technical assistance. This work was supported by USPHS grants R29 CA74230 to JM Lewis, F32 GM18298 to MW Renshaw and P01 HL57900 to MA Schwartz.
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Renshaw, M., Lewis, J. & Schwartz, M. The c-Abl tyrosine kinase contributes to the transient activation of MAP kinase in cells plated on fibronectin. Oncogene 19, 3216–3219 (2000). https://doi.org/10.1038/sj.onc.1203667
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DOI: https://doi.org/10.1038/sj.onc.1203667
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