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Vol. 13, Issue 11, 4060-4073, November 2002
Departments of *Cell Biology and 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 Microscopical
Anatomy, Center of Anatomy, Hannover Medical School, Hannover, Germany
-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.
Corresponding author. E-mail address:
ungewickell.ernst{at}mh-hannover.de.
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