ARF mediates recruitment of PtdIns-4-OH kinase-β and stimulates synthesis of PtdIns(4,5)P2 on the Go
Author: ["Anna Godi","Paolo Pertile","Rachel Meyers","Pierfrancesco Marra","Giuseppe Di Tullio","Cristiano Iurisci","Alberto Luini","Daniela Corda","Maria Antonietta De Matteis"]
Publication: Nature Cell Biology
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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.
Cite this article
Godi, A., Pertile, P., Meyers, R. et al. ARF mediates recruitment of PtdIns-4-OH kinase-β and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex. Nat Cell Biol 1, 280–287 (1999). https://doi.org/10.1038/12993
