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First published online December 1, 2003
doi: 10.1242/10.1242/jcs.00928

Journal of Cell Science 117, 9-18 (2004)
Published by The Company of Biologists 2004
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Commentary

ENTH/ANTH proteins and clathrin-mediated membrane budding

Valerie Legendre-Guillemin*, Sylwia Wasiak*, Natasha K. Hussain, Annie Angers and Peter S. McPherson{ddagger}

Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC H3A 2B4, Canada

{ddagger} Author for correspondence (e-mail: peter.mcpherson{at}mcgill.ca)

The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. Structural analyses and ligand-binding studies have shown that a set of proteins previously designated as harboring an ENTH domain in fact contain a highly similar, yet unique module referred to as an AP180 N-terminal homology (ANTH) domain. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the trans-Golgi network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.

Key words: ENTH domain, ANTH domain, Phosphoinositides, Clathrin-coated vesicle, trans-Golgi network


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