Asymmetric tethering of flat and curved lipid membranes by a golgin.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 18451304.
- Also identified by DOI 10.1126/science.1155821.
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Abstract
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.
Medical subject headings
- Intracellular Membranes
- Membrane Lipids
- Nuclear Proteins