Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission

Jennifer L. Gallop, P. Jonathan G. Butler and Harvey T. McMahon ()
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Jennifer L. Gallop: MRC Laboratory of Molecular Biology
P. Jonathan G. Butler: MRC Laboratory of Molecular Biology
Harvey T. McMahon: MRC Laboratory of Molecular Biology

Nature, 2005, vol. 438, issue 7068, 675-678

Abstract: Abstract Endophilins have been proposed to have an enzymatic activity (a lysophosphatidic acid acyl transferase or LPAAT activity) that can make phosphatidic acid in membranes1,2,3. This activity is thought to change the bilayer asymmetry in such a way that negative membrane curvature at the neck of a budding vesicle will be stabilized. An LPAAT activity has also been proposed for CtBP/BARS (carboxy-terminal binding protein/brefeldin A-ribosylated substrate), a transcription co-repressor that is implicated in dynamin-independent endocytosis and fission of the Golgi in mitosis4,5,6. Here we show that the LPAAT activity associated with endophilin is a contaminant of the purification procedure and can be also found associated with the pleckstrin homology domain of dynamin. Likewise, the LPAAT activity associated with CtBP/BARS is also a co-purification artefact. The proposed locus of activity in endophilins includes the BAR domain, which has no catalytic site but instead senses positive membrane curvature. These data will prompt a re-evaluation of the molecular details of membrane budding.

Date: 2005
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DOI: 10.1038/nature04136

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