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A more recent version of this article appeared on November 1, 2002
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Submitted on March 28, 2002
Revised on August 13, 2002
Accepted on August 21, 2002
1 Department of Cell Biology, Center of Anatomy, Hannover Medical School, D-30623 Hannover, Germany
2 Department of Microscopical Anatomy, Center of Anatomy, Hannover Medical School, D-30623 Hannover, Germany
* Corresponding author. E-mail address: ungewickell.ernst{at}mh-hannover.de.
We have characterized a novel clathrin binding 68 KDa ENTH-domain protein which 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 GGA2, with the appendage domain of ß2-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 more than 17% methionine. Our results suggest that Clint might participate in the formation of clathrin coated vesicles at the level of the TGN and remains associated with the vesicles longer than clathrin and adaptors.
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