Article abstract
Nature Cell Biology 10, 1146 - 1153 (2008)
Published online: 7 September 2008 | doi:10.1038/ncb1774
A role for phosphatidic acid in COPI vesicle fission yields insights into Golgi maintenance
Jia-Shu Yang1, Helge Gad2, Stella Y. Lee1, Alexander Mironov2, Leiliang Zhang1, Galina V. Beznoussenko2, Carmen Valente2, Gabriele Turacchio2, Akua N. Bonsra3, Guangwei Du3, Gianluca Baldanzi4, Andrea Graziani4, Sylvain Bourgoin5, Michael A. Frohman3, Alberto Luini2 & Victor W. Hsu1
Abstract
Proteins essential for vesicle formation by the Coat Protein I (COPI) complex are being identified, but less is known about the role of specific lipids. Brefeldin-A ADP-ribosylated substrate (BARS) functions in the fission step of COPI vesicle formation. Here, we show that BARS induces membrane curvature in cooperation with phosphatidic acid. This finding has allowed us to further delineate COPI vesicle fission into two sub-stages: 1) an earlier stage of bud-neck constriction, in which BARS and other COPI components are required, and 2) a later stage of bud-neck scission, in which phosphatidic acid generated by phospholipase D2 (PLD2) is also required. Moreover, in contrast to the disruption of the Golgi seen on perturbing the core COPI components (such as coatomer), inhibition of PLD2 causes milder disruptions, suggesting that such COPI components have additional roles in maintaining Golgi structure other than through COPI vesicle formation.
- Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115 USA.
- Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy.
- Department of Pharmacology and the Center for Developmental Genetics, Stony Brook University, Stony Brook, NY 11794, USA.
- Department of Clinical and Experimental Medicine, Università del Piemonte Orientale, 28100 Novara, Italy.
- Le Centre Hospitalier Universitaire de Quebec, Pavillon CHUL, Rhumatologie et Immunology, Quebec, Canada G1V4G2.
Correspondence to: Victor W. Hsu1 e-mail: vhsu@rics.bwh.harvard.edu
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