The Remorin C-terminal Anchor was shaped by convergent evolution among membrane binding domains

被引:14
|
作者
Raffaele, Sylvain [1 ]
Perraki, Artemis [2 ]
Mongrand, Sebastien [2 ]
机构
[1] CNRS, INRA, UMR441, LIPM, Castanet Tolosan, France
[2] Univ Bordeaux Segalen, Lab Biogenese Membraniare, UMR 5200, CNRS,INRA,Bordeaux Aquitaine, Villenave Dornon, France
关键词
membrane anchor; lipid rafts; remorin; convergent evolution;
D O I
10.4161/psb.23207
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
StREM1.3 Remorin is a well-established plant raftophilic protein, predominantly associated with sterol-and sphingolipidrich membrane rafts. We recently identified a C-terminal domain (RemCA) required and sufficient for StREM1.3 anchoring to the plasma membrane. Here, we report a search for homologs and analogs of RemCA domain in publicly available protein sequence and structure databases. We could not identify RemCA homologous domains outside the Remorin family but we identified domains sharing bias in amino-acid composition and predicted structural fold with RemCA in bacterial, viral and animal proteins. These results suggest that RemCA emerged by convergent evolution among unrelated membrane binding domain.
引用
收藏
页码:e23207.1 / e23207.4
页数:4
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