Dimerization of Neu/Erb2 transmembrane domain is controlled by membrane curvature

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• 作者：Lucie Khemt¨¦mourian ; S¨¦bastien Buchoux ; Fabien Aussenac and Erick J. Dufourc
• 关键词：Circular dichroism ; Oncogenic peptides ; Bicelle membranes ; 31P ; NMR ; Coiled ; coil interactions
• 刊名：European Biophysics Journal
• 出版年：2007
• 出版时间：February, 2007
• 年：2007
• 卷：36
• 期：2
• 页码：107-112
• 全文大小：660 KB

文摘

Secondary structures of the proto-oncogenic Neu/ErbB2 transmembrane segment and its mutant analogue have been determined in phospholipids. It is found that the mutated peptide possesses less helical character possibly due to the valine/glutamic acid point mutation. Embedding peptides in lipid systems whose topology can change from small (100–200 ?) tumbling objects to bilayer discs of 450 ? diameter leads to the finding that coiled-coil interactions are only observed in the presence of a bilayer membrane of low curvature, independent of mutation. This strongly suggests that any event that may change membrane topology can therefore perturb the dimerization/ologomerization and subsequent phosphorylation cascade leading to cell growth or cancer processes.