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Papers In Press, published online ahead of print May 15, 2003
Department of Neurology and Neurosurgery, McGill University, Montreal, Quebec H3A 2B4
Corresponding Author: peter.mcpherson{at}mcgill.ca
The epsin N-terminal homology (ENTH) domain is a protein module of approximately 150 amino acids found at the N-terminus of a variety of proteins identified in yeast, plants, nematode, frog, and mammals. ENTH domains are comprised of multiple a-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 approximately 1 micromolar 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, epsin 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 AP180 or 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.
J. Biol. Chem, 10.1074/jbc.M300995200
Submitted on January 29, 2003
Revised on May 6, 2003
Accepted on May 15, 2003
A role for ENTH/ANTH domains in tubulin binding
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