Abstract
The small GTPase ADP-ribosylation factor (ARF) regulates the structure and function of the Golgi complex through mechanisms that are understood only in part, and which include an ability to control the assembly of coat complexes and phospholipase D (PLD). Here we describe a new property of ARF, the ability to recruit phosphatidylinositol-4-OH kinase-β and a still unidentified phosphatidylinositol-4-phosphate-5-OH kinase to the Golgi complex, resulting in a potent stimulation of synthesis of phosphatidylinositol-4-phosphate and phosphatidylinositol-4,5-bisphosphate; this ability is independent of its activities on coat proteins and PLD. Phosphatidylinositol-4-OH kinase-β is required for the structural integrity of the Golgi complex: transfection of a dominant-negative mutant of the kinase markedly alters the organization of the organelle.
Original language | English |
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Pages (from-to) | 280-287 |
Number of pages | 8 |
Journal | Nature Cell Biology |
Volume | 1 |
Issue number | 5 |
DOIs | |
Publication status | Published - Sept 1999 |
Externally published | Yes |
Bibliographical note
Funding Information:ACKNOWLEDGEMENTS We thank C. Walch-Solimena and P. Novick for sharing unpublished results; J. Backer, R. Kahn, P. Hauri and F. Wieland for antibodies; J. Moss for the Drosophila ARFIII complementary DNA; M. Falasca for discussions; and C.P. Berrie for critical reading of the manuscript. This work was supported in part by grants from Telethon (E732), the Human Frontier Science Program (to M.A.D.M.), the Italian National Research Council (97.01300. PF49 and 97.01305.PF49) and the Italian Association for Cancer Research. A.G. and P.P. received fellowships from the Centro di Formazione e Studi per il Mezzogiorno (FORMEZ) and Banca di Roma, respectively. Correspondence and requests for materials should be addressed to M.A.D.M.