Tubulation by amphiphysin requires concentration-dependent switching from wedging to scaffolding.
Tubulation by amphiphysin requires concentration-dependent switching from wedging to scaffolding.
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DOI：
10.1016/j.str.2015.02.014
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发表时间：
2015-05-05
期刊：
影响因子：
5.7
通讯作者：
Langen, Ralf
中科院分区：
文献类型：
--
作者：
Isas, J. Mario;Ambroso, Mark R.;Hegde, Prabhavati B.;Langen, Jennifer;Langen, Ralf
BAR proteins are involved in a variety of membrane remodeling events, but how they can mold membranes into different shapes remains poorly understood. Using EPR, we find that vesicle binding of the N-BAR protein amphiphysin is predominantly mediated by the shallow insertion of amphipathic N-terminal helices. In contrast, the interaction with tubes involves deeply inserted N-terminal helices together with the concave surface of the BAR domain, which acts as a scaffold. Combined with the observed concentration dependence of tubulation and BAR domain scaffolding, the data indicate that initial membrane deformations and vesicle binding are mediated by insertion of amphipathic helical wedges, while tubulation requires high protein densities at which oligomeric BAR domain scaffolds form. In addition, we identify a pocket of residues on the concave surface of the BAR domain that deeply insert into tube membrane. Interestingly, this pocket harbors a number of disease mutants in the homologous amphiphysin 2.
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