Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission
Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission
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DOI：
10.1038/nature04136
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发表时间：
2005-12-01
期刊：
影响因子：
64.8
通讯作者：
McMahon, HT
中科院分区：
文献类型：
--
作者：
Gallop, JL;Butler, PJG;McMahon, HT
已提出内亲蛋白具有可在膜中产生磷脂酸的酶活性（溶血磷脂酸酰基转移酶或LPAAT活性）（1-3）。这种活性被认为以这样的方式改变双层的不对称性，即在出芽囊泡的颈部处的负膜曲率将被稳定。还提出了CtBP/ BARS（羧基末端结合蛋白/布雷菲德菌素A-核糖基化底物）的LPAAT活性，CtBP/BARS是一种转录辅阻遏物，涉及有丝分裂中高尔基体的动力蛋白非依赖性内吞作用和分裂（4-6）.在这里，我们表明，LPAAT活性与内啡肽是一种污染物的纯化过程中，也可以发现与pleckstrin同源结构域的发动蛋白。同样，与CtBP/ BARS相关的LPAAT活性也是共纯化假象。提议的内嗜蛋白的活性位点包括BAR结构域，其没有催化位点，而是感知正膜曲率。这些数据将促使重新评估膜出芽的分子细节.
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.