NDLI: Effects of MACPF/CDC proteins on lipid membranes

Content Provider	Springer Nature Link
Author	Gilbert, Robert J. C. Mikelj, Miha Dalla Serra, Mauro Froelich, Christopher J. Anderluh, Gregor
Copyright Year	2012
Abstract	Recent work on the MACPF/CDC superfamily of pore-forming proteins has focused on the structural analysis of monomers and pore-forming oligomeric complexes. We set the family of proteins in context and highlight aspects of their function which the direct and exclusive equation of oligomers with pores fails to explain. Starting with a description of the distribution of MACPF/CDC proteins across the domains of life, we proceed to show how their evolutionary relationships can be understood on the basis of their structural homology and re-evaluate models for pore formation by perforin, in particular. We furthermore highlight data showing the role of incomplete oligomeric rings (arcs) in pore formation and how this can explain small pores generated by oligomers of proteins belonging to the family. We set this in the context of cell biological and biophysical data on the proteins’ function and discuss how this helps in the development of an understanding of how they act in processes such as apicomplexan parasites gliding through cells and exiting from cells.
Starting Page	2083
Ending Page	2098
Page Count	16
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	70
Issue Number	12
e-ISSN	14209071
Language	English
Publisher	SP Birkhäuser Verlag Basel
Publisher Date	2012-09-15
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	MACPF domain Cholesterol-dependent cytolysins Pore Membrane interactions Membrane damage Cell Biology Biomedicine general Life Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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