The m1 muscarinic acetylcholine receptor transactivates the EGF receptor to modulate ion channel activity - PubMed (original) (raw)

The m1 muscarinic acetylcholine receptor transactivates the EGF receptor to modulate ion channel activity

W Tsai et al. EMBO J. 1997.

Abstract

Intracellular tyrosine kinases link the G protein-coupled m1 muscarinic acetylcholine receptor (mAChR) to multiple cellular responses. However, the mechanisms by which m1 mAChRs stimulate tyrosine kinase activity and the identity of the kinases within particular signaling pathways remain largely unknown. We show that the epidermal growth factor receptor (EGFR), a single transmembrane receptor tyrosine kinase, becomes catalytically active and dimerized through an m1 mAChR-regulated pathway that requires protein kinase C, but is independent of EGF. Finally, we demonstrate that transactivation of the EGFR plays a major role in a pathway linking m1 mAChRs to modulation of the Kv1.2 potassium channel. These results demonstrate a ligand-independent mechanism of EGFR transactivation by m1 mAChRs and reveal a novel role for these growth factor receptors in the regulation of ion channels by G protein-coupled receptors.

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References

    1. J Biol Chem. 1984 Feb 25;259(4):2553-8 - PubMed
    1. J Biol Chem. 1997 Feb 14;272(7):4637-44 - PubMed
    1. J Biol Chem. 1985 Nov 25;260(27):14538-46 - PubMed
    1. Biochemistry. 1987 Mar 10;26(5):1443-51 - PubMed
    1. Mol Cell Biol. 1987 Dec;7(12):4568-71 - PubMed

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