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

Abstract

StREM1.3 Remorin is a well-established plant raftophilic protein, predominantly associated with sterol- and sphingolipid-rich 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.

Keywords: :

• membrane anchor
• lipid rafts
• remorin
• convergent evolution

Disclosure of Potential Conflicts of Interest

No potential conflicts of interest were disclosed.

Acknowledgments

This work was supported by the French Agence Nationale pour la Recherche (contract no. NT09_517917 PANACEA) to S.M.