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Vol. 16, Issue 8, 3692-3704, August 2005
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Is a Component of Adaptor Protein-3-derived Vesicles
* Department of Cell Biology, Emory University, Atlanta, GA 30322;
Department of Pathology and Laboratory Medicine, Emory University, Atlanta, GA 30322;
Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, GA 30322;
¶ Center for Neurodegenerative Disease, Emory University, Atlanta, GA 30322; and
|| Howard Hughes Medical Institute and Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510
Submitted January 10, 2005;
Revised May 11, 2005;
Accepted May 31, 2005
Monitoring Editor: Keith Mostov
A membrane fraction enriched in vesicles containing the adaptor protein (AP) -3 cargo zinc transporter 3 was generated from PC12 cells and was used to identify new components of these organelles by mass spectrometry. Proteins prominently represented in the fraction included AP-3 subunits, synaptic vesicle proteins, and lysosomal proteins known to be sorted in an AP-3-dependent way or to interact genetically with AP-3. A protein enriched in this fraction was phosphatidylinositol-4-kinase type II
(PI4KII). Biochemical, pharmacological, and morphological analyses supported the presence of PI4KII in AP-3-positive organelles. Furthermore, the subcellular localization of PI4KII was altered in cells from AP-3-deficient mocha mutant mice. The PI4KII normally present both in perinuclear and peripheral organelles was substantially decreased in the peripheral membranes of AP-3-deficient mocha fibroblasts. In addition, as is the case for other proteins sorted in an AP-3-dependent way, PI4KII content was strongly reduced in nerve terminals of mocha hippocampal mossy fibers. The functional relationship between AP-3 and PI4KII was further explored by PI4KII knockdown experiments. Reduction of the cellular content of PI4KII strongly decreased the punctate distribution of AP-3 observed in PC12 cells. These results indicate that PI4KII is present on AP-3 organelles where it regulates AP-3 function.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
These authors contributed equally to this work.
Address correspondence to: Victor Faundez (faundez{at}cellbio.emory.edu).
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