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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ADP-Ribosylation Factor 1 / metabolism
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Binding Sites
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Cell Line
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Cytoskeletal Proteins
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GTPase-Activating Proteins / metabolism
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Golgi Apparatus / chemistry
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Golgi Apparatus / metabolism
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HeLa Cells
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Humans
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Intracellular Membranes / chemistry*
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Intracellular Membranes / metabolism
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Liposomes
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Membrane Lipids / chemistry*
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
Substances
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ARFGAP1 protein, human
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ARFGAP3 protein, human
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Cytoskeletal Proteins
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GTPase-Activating Proteins
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Liposomes
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Membrane Lipids
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Nuclear Proteins
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Recombinant Proteins
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TRIP11 protein, human
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ADP-Ribosylation Factor 1