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J. Biol. Chem., Vol. 278, Issue 31, 28823-28830, August 1, 2003

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A Role for Epsin N-terminal Homology/AP180 N-terminal Homology (ENTH/ANTH) Domains in Tubulin Binding^*

Natasha K. Hussain  , Montarop Yamabhai ¶, Asha L. Bhakar  ||, Martina Metzler **, Stephen S. G. Ferguson , Michael R. Hayden **, Peter S. McPherson   and Brian K. Kay ¶¶

From the Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada, ^¶School of Biotechnology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand, ^**The Centre for Molecular Medicine and Therapeutics, Department of Medical Genetics, University of British Columbia, Vancouver, British Columbia V5Z 4H4, Canada, Cell Biology Research Group, Robarts Research Institute, London, Ontario N6A 5K8, Canada, and ^¶¶Biosciences Division, Argonne National Laboratory, Argonne, Illinois 60439

The epsin N-terminal homology (ENTH) domain is a protein module of 150 amino acids found at the N terminus of a variety of proteins identified in yeast, plants, nematode, frog, and mammals. ENTH domains comprise multiple -helices folded upon each other to form a compact globular structure that has been implicated in interactions with lipids and proteins. In characterizing this evolutionarily conserved domain, we isolated and identified tubulin as an ENTH domain-binding partner. The interaction, which is direct and has a dissociation constant of 1 µM, was observed with ENTH domains of proteins present in various species. Tubulin is co-immunoprecipitated from rat brain extracts with the ENTH domain-containing proteins, epsins 1 and 2, and punctate epsin staining is observed along the microtubule cytoskeleton of dissociated cortical neurons. Consistent with a role in microtubule processes, the over-expression of epsin ENTH domain in PC12 cells stimulates neurite outgrowth. These data demonstrate an evolutionarily conserved property of ENTH domains to interact with tubulin and microtubules.

Received for publication, January 29, 2003 , and in revised form, May 6, 2003.

Note Added in Proof—Rappoport et al. (Rappoport, J. Z., Taha, B. W., and Simon, S. M. (2003) Traffic 4, 460–467) have recently reported the lateral movement of plasma membrane-associated dsRed-clathrin spots along microtubules parallel to the plasma membrane.

^* This work was generously supported by Grant 197685 from the Natural Sciences and Engineering Research Council (to P. S. M.), the Canadian Institutes of Health Research (CIHR) (to M. R. H.), and Merck-Frosst Canada (to M. R. H. and M. M). 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 a studentship from the Fond de la Recherche en Sante du Quebec.

^|| Supported by a studentship from the CIHR.

A CIHR Investigator, a Killam Scholar of the Montreal Neurological Institute, and a McGill University William Dawson Scholar. To whom correspondence should be addressed: Dept. of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, 3801 University Ave., Montreal, Quebec H3A 2B4, Canada. Tel.: 514-398-7355; Fax: 514-398-8106; E-mail: peter.mcpherson{at}mcgill.ca.

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