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Vol. 13, Issue 11, 4060-4073, November 2002

Clint: A Novel Clathrin-binding ENTH-Domain Protein at the Golgi

Christoph Kalthoff,^* Stephanie Groos, Rüdiger Kohl,^* Stefan Mahrhold,^* and Ernst J. Ungewickell^*

Departments of  ^*Cell Biology and  Microscopical Anatomy, Center of Anatomy, Hannover Medical School, Hannover, Germany

We have characterized a novel clathrin-binding 68-kDa epsin N-terminal homology domain (ENTH-domain) protein that we name clathrin interacting protein localized in the trans-Golgi region (Clint). It localizes predominantly to the Golgi region of epithelial cells as well as to more peripheral vesicular structures. Clint colocalizes with AP-1 and clathrin only in the perinuclear area. Recombinantly expressed Clint interacts directly with the -appendage domain of AP-1, with the clathrin N-terminal domain through the peptide motif ⁴²³LFDLM, with the -adaptin ear homology domain of Golgi-localizing, -adaptin ear homology domain 2, with the appendage domain of 2-adaptin and to a lesser extent with the appendage domain of -adaptin. Moreover, the Clint ENTH-domain asssociates with phosphoinositide-containing liposomes. A significant amount of Clint copurifies with rat liver clathrin-coated vesicles. In rat kidney it is preferentially expressed in the apical region of epithelial cells that line the collecting duct. Clathrin and Clint also colocalize in the apical region of enterocytes along the villi of the small intestine. Apart from the ENTH-domain Clint has no similarities with the epsins AP180/CALM or Hip1/1R. A notable feature of Clint is a carboxyl-terminal methionine-rich domain (Met⁴²⁷-Met⁶⁰⁵), which contains >17% methionine. Our results suggest that Clint might participate in the formation of clathrin-coated vesicles at the level of the trans-Golgi network and remains associated with the vesicles longer than clathrin and adaptors.

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Corresponding author. E-mail address: ungewickell.ernst{at}mh-hannover.de.

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Molecular Biology of the Cell
Vol. 13, 4060-4073, November 2002
Copyright © 2002 by The American Society for Cell Biology

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