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Originally published In Press as doi:10.1074/jbc.M302865200 on May 8, 2003

J. Biol. Chem., Vol. 278, Issue 31, 28993-28999, August 1, 2003
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Contrasting Membrane Interaction Mechanisms of AP180 N-terminal Homology (ANTH) and Epsin N-terminal Homology (ENTH) Domains*

Robert V. Stahelin {ddagger}, Fei Long {ddagger}, Brian J. Peter § ¶, Diana Murray ||, Pietro De Camilli **, Harvey T. McMahon § and Wonhwa Cho {ddagger} {ddagger}{ddagger}

From the {ddagger}Department of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, the §Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom, the ||Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10021, and the **Howard Hughes Medical Institute and Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510

Epsin and AP180/CALM are endocytotic accessory proteins that have been implicated in the formation of clathrin-coated pits. Both proteins have phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-binding domains in their N termini, but these domains are structurally and functionally different. To understand the basis of their distinct properties, we measured the PtdIns(4,5)P2-dependent membrane binding of the epsin N-terminal homology (ENTH) domain and the AP180 N-terminal homology (ANTH) domain by means of surface plasmon resonance and monolayer penetration techniques and also calculated the effect of PtdIns(4,5)P2 on the electrostatic potential of these domains. PtdIns(4,5)P2 enhances the electrostatic membrane association of both domains; however, PtdIns(4,5)P2 binding exerts distinct effects on their membrane dissociation. Specifically, PtdIns(4,5)P2 induces the membrane penetration of the N-terminal {alpha}-helix of the ENTH domain, which slows the membrane dissociation of the domain and triggers the membrane deformation. These results provide the biophysical explanation for the membrane bending activity of epsin and its ENTH domain.

Received for publication, March 20, 2003 , and in revised form, May 8, 2003.

* This work was supported by National Institutes of Health Grants GM66147 (to D. M.) and GM52598 and GM53987 (to W. C.). 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.

Supported by an European Molecular Biology Long Term Postdoctoral Fellowship.

{ddagger}{ddagger} To whom correspondence should be addressed: Dept. of Chemistry (M/C 111), University of Illinois at Chicago, 845 West Taylor St., Chicago, IL 60607-7061. Tel.: 312-996-4883; Fax: 312-996-2183; E-mail: wcho{at}uic.edu.


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