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MBC in Press, published online ahead of print August 16, 2006
Mol. Biol. Cell 10.1091/mbc.E06-05-0390

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Submitted on May 4, 2006
Revised on August 2, 2006
Accepted on August 3, 2006

Clathrin-dependent Association of CVAK104 with Endosomes and the Trans-Golgi Network

Michael Düwel and Ernst J. Ungewickell

Department of Cell Biology, Center of Anatomy, Hannover Medical School, D-30625 Hannover, Germany

Monitoring Editor: Jean Gruenberg

CVAK104 is a novel clathrin-coated vesicle associated protein that was recently shown to phosphorylate the {beta}2-subunit of the adaptor complex AP2 in vitro (Conner and Schmid, 2005). Here, we demonstrate that a C-terminal segment of CVAK104 interacts with the N-terminal domain of clathrin and with the {alpha}-appendage of AP2. CVAK104 localizes predominantly to the perinuclear region of HeLa and COS-7 cells but it is also present on peripheral vesicular structures that are accessible to endocytosed transferrin. The distribution of CVAK104 overlaps extensively with that of AP1, AP3, the mannose 6-phosphate receptor and clathrin but not at all with its putative phosphorylation target AP2. RNAi-mediated clathrin knockdown reduced the membrane association of CVAK104. Recruitment of CVAK104 to perinuclear membranes of permeabilized cells is enhanced by GTP{gamma}S, and Brefeldin A redistributes CVAK104 in cells. Both observations suggest a direct or indirect requirement for GTP-binding proteins in the membrane association of CVAK104. Live-cell imaging showed colocalization of GFP-CVAK104 with endocytosed transferrin and with RFP-clathrin on rapidly moving endosomes. Like AP1-depleted COS-7 cells, CVAK104-depleted cells missort the lysosomal hydrolase cathepsin D. Taken together our data suggest a function for CVAK104 in clathrin-dependent pathways between the trans-Golgi network and the endosomal system.

Address correspondence to: Ernst J. Ungewickell (ungewickell.ernst{at}mh-hannover.de)




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