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Asymmetric tethering of flat and curved lipid membranes by a golgin.

Drin G, Morello V, Casella JF, Gounon P, Antonny B.

Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France.

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.

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PMID: 18451304 [PubMed - indexed for MEDLINE]