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Originally published as MBC in Press, 10.1091/mbc.E05-01-0042 on March 30, 2005

Vol. 16, Issue 6, 2786-2798, June 2005

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Association of the Leukocyte Plasma Membrane with the Actin Cytoskeleton through Coiled Coil-mediated Trimeric Coronin 1 Molecules

John Gatfield * {dagger} {ddagger}, Imke Albrecht * {dagger}, Bettina Zanolari *, Michel O. Steinmetz §, and Jean Pieters *

* Biozentrum, University of Basel, CH 4056 Basel, Switzerland; § Biomolecular Research, Structural Biology, Paul Scherrer Institut, CH 5232 Villigen, Switzerland

Submitted January 18, 2005; Revised March 11, 2005; Accepted March 19, 2005
Monitoring Editor: Paul Matsudaira

Coronin 1 is a member of the coronin protein family specifically expressed in leukocytes and accumulates at sites of rearrangements of the F-actin cytoskeleton. Here, we describe that coronin 1 molecules are coiled coil-mediated homotrimeric complexes, which associate with the plasma membrane and with the cytoskeleton via two distinct domains. Association with the cytoskeleton was mediated by trimerization of a stretch of positively charged residues within a linker region between the N-terminal, WD repeat-containing domain and the C-terminal coiled coil. In contrast, neither the coiled coil nor the positively charged residues within the linker domain were required for plasma membrane binding, suggesting that the N-terminal, WD repeat-containing domain mediates membrane interaction. The capacity of coronin 1 to link the leukocyte cytoskeleton to the plasma membrane may serve to integrate outside-inside signaling with modulation of the cytoskeleton.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–01–0042) on March 30, 2005.

{dagger} These authors contributed equally to this study.

{ddagger} Present address: Actelion Pharmaceuticals, Gewerbestr. 16, CH 4123 Allschwil, Switzerland.

Address correspondence to: Jean Pieters (jean.pieters{at}unibas.ch).




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