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J. Biol. Chem., Vol. 278, Issue 26, 23233-23242, June 27, 2003

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Two Different Heparin-binding Domains in the Triple-helical Domain of ColQ, the Collagen Tail Subunit of Synaptic Acetylcholinesterase^*

Paola Deprez   ¶, Nibaldo C. Inestrosa  and Eric Krejci 

From the Centro de Regulación Celular y Patología Dr. Joaquín V. Luco, Instituto Milenio de Biología Fundamental y Aplicada, Facultad de Ciencias Biológicas, P. Universidad Católica de Chile, Casilla 114-D, Santiago, Chile and Laboratoire de Neurobiologie Cellulaire et Moléculaire, CNRS Unité Mixte de Recherche 8544, Ecole Normale Supérieure, 75230 Paris Cedex 05, France

ColQ, the collagen tail subunit of asymmetric acetylcholinesterase, is responsible for anchoring the enzyme at the vertebrate synaptic basal lamina by interacting with heparan sulfate proteoglycans. To get insights about this function, the interaction of ColQ with heparin was analyzed. For this, heparin affinity chromatography of the complete oligomeric enzyme carrying different mutations in ColQ was performed. Results demonstrate that only the two predicted heparin-binding domains present in the collagen domain of ColQ are responsible for heparin interaction. Despite their similarity in basic charge distribution, each heparin-binding domain had different affinity for heparin. This difference is not solely determined by the number or nature of the basic residues conforming each site, but rather depends critically on local structural features of the triple helix, which can be influenced even by distant regions within ColQ. Thus, ColQ possesses two heparin-binding domains with different properties that may have non-redundant functions. We hypothesize that these binding sites coordinate acetylcholinesterase positioning within the organized architecture of the neuromuscular junction basal lamina.

Received for publication, February 7, 2003 , and in revised form, April 7, 2003.

^* This work was supported by Fondo Nacional de Ciencia y Tecnología Grant 2970072 (to P. D.), Fondo de Investigación Avanzada en Areas Prioritarias Grant 3980001, and by the Millennium Institute for Fundamental and Applied Biology (to N. C. I.), the CNRS, and the Association Française contre les Myopathies. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Present address: Institut für Biochemie, ETH-Hönggerberg HPM1, 8093 Zürich, Switzerland. To whom correspondence should be addressed. Tel.: 41-1-632-69-01; Fax: 41-1-632-12-69; E-mail: paola.deprez{at}bc.biol.ethz.ch.

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