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Vol. 19, Issue 4, 1415-1426, April 2008

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Phosphatidylinositol-4-Kinase Type II Alpha Contains an AP-3–sorting Motif and a Kinase Domain That Are Both Required for Endosome Traffic

Branch Craige^*,, Gloria Salazar, and Victor Faundez^,

*Graduate Program in Biochemistry, Cell, and Developmental Biology, and Department of Cell Biology, and Center for Neurodegenerative Diseases, Emory University, Atlanta, GA 30322

Submitted December 12, 2007; Revised January 9, 2008; Accepted January 25, 2008
Monitoring Editor: Sandra Lemmon

InCytes from MBC

The adaptor complex 3 (AP-3) targets membrane proteins from endosomes to lysosomes, lysosome-related organelles and synaptic vesicles. Phosphatidylinositol-4-kinase type II (PI4KII) is one of several proteins possessing catalytic domains that regulate AP-3–dependent sorting. Here we present evidence that PI4KII uniquely behaves both as a membrane protein cargo as well as an enzymatic regulator of adaptor function. In fact, AP-3 and PI4KII form a complex that requires a dileucine-sorting motif present in PI4KII. Mutagenesis of either the PI4KII-sorting motif or its kinase-active site indicates that both are necessary to interact with AP-3 and properly localize PI4KII to LAMP-1–positive endosomes. Similarly, both the kinase activity and the sorting signal present in PI4KII are necessary to rescue endosomal PI4KII siRNA-induced mutant phenotypes. We propose a mechanism whereby adaptors use canonical sorting motifs to selectively recruit a regulatory enzymatic activity to restricted membrane domains.

Address correspondence to: Victor Faundez (faundez{at}cellbio.emory.edu)

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InCytes from MBC, April 2008

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