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First published online 21 March 2006
doi: 10.1242/jcs.02872

Journal of Cell Science 119, 1528-1536 (2006)
Published by The Company of Biologists 2006
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Research Article

Stimulation of G{alpha}q-coupled M1 muscarinic receptor causes reversible spectrin redistribution mediated by PLC, PKC and ROCK

Miyoko Street1,*, Stephen J. Marsh2, Paul R. Stabach3, Jon S. Morrow3, David A. Brown2 and Noel J. Buckley1

1 University of Leeds, Institute of Membrane and Systems Biology, Garstang Building, Mount Preston Street, Leeds LS2 9JT, UK
2 Department of Pharmacology, University College London, Gower Street, London, WC1E 6BT, UK
3 Department of Pathology, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06520, USA

* Author for correspondence (e-mail: m.street{at}bmb.leeds.ac.uk)

Accepted 4 January 2006

Spectrin is a cytoskeletal protein that plays a role in formation of the specialized plasma membrane domains. However, little is known of the molecular mechanism that regulates responses of spectrin to extracellular stimuli, such as activation of G-protein-coupled receptor (GPCR). We have found that {alpha}II spectrin is a component of the G{alpha}q/11-associated protein complex in CHO cells stably expressing the M1 muscarinic receptor, and investigated the effect of activation of GPCR on the cellular localization of yellow-fluorescent-protein-tagged {alpha}II spectrin. Stimulation of G{alpha}q/11-coupled M1 muscarinic receptor triggered reversible redistribution of {alpha}II spectrin following a rise in intracellular Ca2+ concentration. This redistribution, accompanied by non-apoptotic membrane blebbing, required an intact actin cytoskeleton and was dependent on activation of phospholipase C, protein kinase C, and Rho-associated kinase ROCK. Muscarinic-agonist-induced spectrin remodeling appeared particularly active at localized domains, which is clear contrast to that caused by constitutive activation of ROCK and to global rearrangement of the spectrin lattice caused by changes in osmotic pressure. These results suggest a role for spectrin in providing a dynamic and reversible signaling platform to the specific domains of the plasma membrane in response to stimulation of GPCR.

Key words: {alpha}II spectrin, Membrane-skeleton remodeling, G{alpha}q-coupled receptor signaling, Signaling complex, Rho-associated kinase






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