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J Biol Chem, Vol. 273, Issue 14, 8344-8350, April 3, 1998

Specific Interaction of Golgi Coatomer Protein -COP with Phosphatidylinositol 3,4,5-Trisphosphate

Anu Chaudhary^§, Qu-Ming Gu^§, Oliver Thum^§, Adam A. Profit^§, Ying Qi^¶, Loice Jeyakumar^¶, Sidney Fleischer^¶, and Glenn D. Prestwich^§

From  The University of Utah, Department of Medicinal Chemistry, Salt Lake City, Utah 84112-5820, the ^§ Departments of Chemistry and Biochemistry and Cell Biology, The University at Stony Brook, Stony Brook, New York 11794-3400, and the ^¶ Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235

The phosphoinositide binding selectivity of Golgi coatomer COPI polypeptides was examined using photoaffinity analogs of the soluble inositol polyphosphates Ins(1,4,5)P₃, Ins(1,3,4,5)P₄, and InsP₆, and of the polyphosphoinositides PtdIns(3,4,5)P₃, PtdIns(4,5)P₂, and PtdIns(3,4)P₂. Highly selective Ins(1,3,4,5)P₄-displaceable photocovalent modification of the -COP subunit was observed with a p-benzoyldihydrocinnamide (BZDC)-containing probe, [³H]BZDC-Ins(1,3,4,5)P₄. A more highly phosphorylated probe, [³H]BZDC-InsP₆ probe labeled six of the seven subunits, with only , ', , and -COP showing competitive displacement by excess InsP₆. Importantly, [³H]BZDC-triester-PtdIns(3,4,5)P₃, the lipid with the same phosphorylation pattern as Ins(1,3,4,5)P₄, showed specific, PtdIns(3,4,5)P₃-displaceable labeling of only -COP. Labeling by the PtdIns(4,5)P₂ and PtdIns(3,4)P₂ photoaffinity probes was less intense and showed no discrimination based on PtdInsP_n ligand. Thus, both the D-3 and D-5 phosphates are critical for the -COP-PtdIns(3,4,5)P₃ interaction, suggesting an important role for this polyphosphoinositide in vesicular trafficking.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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