Journal
NATURE
Volume 438, Issue 7068, Pages 675-678Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature04136
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Endophilins have been proposed to have an enzymatic activity ( a lysophosphatidic acid acyl transferase or LPAAT activity) that can make phosphatidic acid in membranes(1-3). 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 mitosis(4-6). 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.
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