4.5 Article Proceedings Paper

Lysenin: A sphingomyelin specific pore-forming toxin

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1780, Issue 3, Pages 612-618

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2007.09.001

Keywords

lipid domain; lipid rafts; cholesterol; glycolipids

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Sphingomyclin is a major sphingolipid in mammalian cells. Recent results indicate that sphingomyelin is a reservoir of lipid second messengers, ceramide and sphingosine-1 -phosphate. Sphingomyelin is also a major component of sphingolipid and cholesterol-rich membrane domains (lipid rafts). Lysenin is a pore-forming toxin that specifically binds sphingomyelin. The binding of lysenin to sphingomyelin is dependent on the membrane distribution of the lipid, i.e. the toxin selectively binds sphingomyclin clusters. Development of a non-toxic lysenin mutant revealed the spatial and functional heterogeneity of sphingolipid-rich membrane domains. (C) 2007 Elsevier B.V. All rights reserved.

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