TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 277, No. 41, Issue of October 11, pp. 38596 –38606, 2002 © 2002 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Tyrosine Phosphorylation of Kv1.2 Modulates Its Interaction with the Actin-binding Protein Cortactin* Received for publication, May 21, 2002, and in revised form, July 29, 2002 Published, JBC Papers in Press, July 31, 2002, DOI 10.1074/jbc.M205005200 David Hattan, Edmund Nesti, Teresa G. Cachero‡, and Anthony D. Morielli§ From the Department of Pharmacology, University of Vermont College of Medicine, Burlington, Vermont 04505 Tyrosine phosphorylation evokes functional changes Kv1.2 
-subunit protein becomes tyrosine-phosphorylated upon the activation of M1 muscarinic acetylcholine receptors in a variety of ion channels. Modulation of the actin cytoskeleton also affects the function of some channels. (mAChRs), leading to a profound suppression of Kv1.2 ionic Little is known about how these avenues of ion channel current (14). Part of the mechanism for such suppression in- regulation may interact. We report that the potassium volves phosphorylation of the N-terminal tyrosine Tyr . How- channel Kv1.2 associates with the actin-binding protein ever, phosphorylation of additional tyrosines within Kv1.2 is cortactin and that the binding is modulated by tyrosine also 
TI - Tyrosine Phosphorylation of Kv1.2 Modulates Its Interaction with the Actin-binding Protein Cortactin
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.m205005200
DA - 2002-10-01
UR - https://www.deepdyve.com/lp/unpaywall/tyrosine-phosphorylation-of-kv1-2-modulates-its-interaction-with-the-NhoJ5wzqUB
DP - DeepDyve
ER -