Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 2 May 2008:
Vol. 320. no. 5876, pp. 670 - 673
DOI: 10.1126/science.1155821
Prev | Table of Contents | Next

Reports

Asymmetric Tethering of Flat and Curved Lipid Membranes by a Golgin

Guillaume Drin,1 Vincent Morello,1 Jean-François Casella,1 Pierre Gounon,2 Bruno Antonny1*

Golgins, long stringlike proteins, tether cisternae and transport vesicles at the Golgi apparatus. We examined the attachment of golgin GMAP-210 to lipid membranes. GMAP-210 connected highly curved liposomes to flatter ones. This asymmetric tethering relied on motifs that sensed membrane curvature both in the N terminus of GMAP-210 and in ArfGAP1, which controlled the interaction of the C terminus of GMAP-210 with the small guanine nucleotide–binding protein Arf1. Because membrane curvature constantly changes during vesicular trafficking, this mode of tethering suggests a way to maintain the Golgi architecture without compromising membrane flow.

1 Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France.
2 Centre Commun de Microscopie Appliquée, Parc Valrose, 06108 Nice Cedex 2, France.

* To whom correspondence should be addressed. E-mail: antonny{at}ipmc.cnrs.fr

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Vps41 Phosphorylation and the Rab Ypt7 Control the Targeting of the HOPS Complex to Endosome-Vacuole Fusion Sites.
M. Cabrera, C. W. Ostrowicz, M. Mari, T. J. LaGrassa, F. Reggiori, and C. Ungermann (2009)
Mol. Biol. Cell 20, 1937-1948
   Abstract »    Full Text »    PDF »
A Primary Role for Golgi Positioning in Directed Secretion, Cell Polarity, and Wound Healing.
S. Yadav, S. Puri, and A. D. Linstedt (2009)
Mol. Biol. Cell 20, 1728-1736
   Abstract »    Full Text »    PDF »
Mechanisms of transport through the Golgi complex.
C. L. Jackson (2009)
J. Cell Sci. 122, 443-452
   Abstract »    Full Text »    PDF »
Discrete Determinants in ArfGAP2/3 Conferring Golgi Localization and Regulation by the COPI Coat.
L. Kliouchnikov, J. Bigay, B. Mesmin, A. Parnis, M. Rawet, N. Goldfeder, B. Antonny, and D. Cassel (2009)
Mol. Biol. Cell 20, 859-869
   Abstract »    Full Text »    PDF »
Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking.
C. Weimer, R. Beck, P. Eckert, I. Reckmann, J. Moelleken, B. Brugger, and F. Wieland (2008)
J. Cell Biol. 183, 725-735
   Abstract »    Full Text »    PDF »
COPI coat assembly occurs on liquid-disordered domains and the associated membrane deformations are limited by membrane tension.
J.-B. Manneville, J.-F. Casella, E. Ambroggio, P. Gounon, J. Bertherat, P. Bassereau, J. Cartaud, B. Antonny, and B. Goud (2008)
PNAS 105, 16946-16951
   Abstract »    Full Text »    PDF »
HELIQUEST: a web server to screen sequences with specific {alpha}-helical properties.
R. Gautier, D. Douguet, B. Antonny, and G. Drin (2008)
Bioinformatics 24, 2101-2102
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)