期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1858, 期 3, 页码 457-466出版社
ELSEVIER
DOI: 10.1016/j.bbamem.2015.09.013
关键词
Pore forming proteins (PFPs); Pore forming toxins (PFTs); Protein oligomerization; Pore structure; Membrane
资金
- Max Planck Society
- Bundesministerium fur Bildung and Forschung [N.0312040]
- European Research Council [ERC-2012-StG-309966]
- Deutsche Forschungsgemeinschaft (DFG) [FOR2036]
- Institutional Strategy of the University of Tubingen (Deutsche Forschungsgemeinschaft) [ZUK 63]
- Alexander von Humboldt Foundation
Pore forming proteins (PFPs) share the ability of creating pores that allow the passage of ions, proteins or other constituents through a wide variety of target membranes, ranging from bacteria to humans. They often cause cell death, as pore formation disrupts the membrane permeability barrier required for maintaining cell homeostasis. The organization into supramolecular complexes or oligomers that pierce the membrane is a common feature of PFPs. However, the molecular pathway of self-assembly and pore opening remains unclear. Here, we review the most recent discoveries in the mechanism of membrane oligomerization and pore formation of a subset of PFPs, the alpha-PFPs, whose pore-forming domains are formed by helical segments. Only now we are starting to grasp the molecular details of their function, mainly thanks to the introduction of single molecule microscopy and nanoscopy techniques. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale. (C) 2015 Elsevier B.V. All rights reserved.
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