1. Phosphatidylinositol 4-Kinaseβ Is Critical for Functional Association of rab11 with the Golgi Complex
- Author
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Niels Geijsen, Bart M. Gadella, Paul J. Coffer, Paul M.P. van Bergen en Henegouwen, Petra de Graaf, Peter van der Sluijs, Thomas K.F. Schulz, Arie J. Verkleij, Remco A.J. van Dijken, Magdalena Deneka, and Wilbert Zwart
- Subjects
DNA, Complementary ,Endosome ,Green Fluorescent Proteins ,Golgi Apparatus ,Saccharomyces cerevisiae ,Biology ,Transfection ,Cell membrane ,symbols.namesake ,chemistry.chemical_compound ,Viral Envelope Proteins ,Cricetinae ,Two-Hybrid System Techniques ,medicine ,Animals ,Phosphatidylinositol ,Molecular Biology ,Secretory pathway ,Glutathione Transferase ,Binding Sites ,Brefeldin A ,Membrane Glycoproteins ,Cell Membrane ,Biological Transport ,DNA ,Articles ,Cell Biology ,COPI ,Golgi apparatus ,beta-Galactosidase ,Protein Structure, Tertiary ,Cell biology ,Luminescent Proteins ,Phosphotransferases (Alcohol Group Acceptor) ,medicine.anatomical_structure ,Microscopy, Fluorescence ,chemistry ,Biochemistry ,rab GTP-Binding Proteins ,COS Cells ,symbols ,Guanosine Triphosphate ,Protein Binding ,PI4KB - Abstract
Phosphatidylinositol 4-kinasebeta (PI4Kbeta) plays an essential role in maintaining the structural integrity of the Golgi complex. In a search for PI4Kbeta-interacting proteins, we found that PI4Kbeta specifically interacts with the GTP-bound form of the small GTPase rab11. The PI4Kbeta-rab11 interaction is of functional significance because inhibition of rab11 binding to PI4Kbeta abolished the localization of rab11 to the Golgi complex and significantly inhibited transport of vesicular stomatitis virus G protein from the Golgi complex to the plasma membrane. We propose that a novel function of PI4Kbeta is to act as a docking protein for rab11 in the Golgi complex, which is important for biosynthetic membrane transport from the Golgi complex to the plasma membrane.
- Published
- 2004