Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 475-486 |
| Number of pages | 12 |
| Journal | Biochimica et Biophysica Acta - Biomembranes |
| Volume | 1858 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1 Mar 2016 |
Keywords
- MACPF
- CDC
- Pore forming toxin
- Perforin
- Membrane attack complex
- Pleurotolysin
Cite this
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Giant MACPF/CDC pore forming toxins : A class of their own. / Reboul, Cyril F; Whisstock, James C; Dunstone, Michelle A.
In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1858, No. 3, 01.03.2016, p. 475-486.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Giant MACPF/CDC pore forming toxins
T2 - A class of their own
AU - Reboul, Cyril F
AU - Whisstock, James C
AU - Dunstone, Michelle A
PY - 2016/3/1
Y1 - 2016/3/1
N2 - Pore Forming Toxins (PFTs) represent a key mechanism for permitting the passage of proteins and small molecules across the lipid membrane. These proteins are typically produced as soluble monomers that self-assemble into ring-like oligomeric structures on the membrane surface. Following such assembly PFTs undergo a remarkable conformational change to insert into the lipid membrane. While many different protein families have independently evolved such ability, members of the Membrane Attack Complex PerForin/Cholesterol Dependent Cytolysin (MACPF/CDC) superfamily form distinctive giant beta-barrel pores comprised of up to 50 monomers and up to 300A in diameter. In this review we focus on recent advances in understanding the structure of these giant MACPF/CDC pores as well as the underlying molecular mechanisms leading to their formation. Commonalities and evolved variations of the pore forming mechanism across the superfamily are discussed. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale.
AB - Pore Forming Toxins (PFTs) represent a key mechanism for permitting the passage of proteins and small molecules across the lipid membrane. These proteins are typically produced as soluble monomers that self-assemble into ring-like oligomeric structures on the membrane surface. Following such assembly PFTs undergo a remarkable conformational change to insert into the lipid membrane. While many different protein families have independently evolved such ability, members of the Membrane Attack Complex PerForin/Cholesterol Dependent Cytolysin (MACPF/CDC) superfamily form distinctive giant beta-barrel pores comprised of up to 50 monomers and up to 300A in diameter. In this review we focus on recent advances in understanding the structure of these giant MACPF/CDC pores as well as the underlying molecular mechanisms leading to their formation. Commonalities and evolved variations of the pore forming mechanism across the superfamily are discussed. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale.
KW - MACPF
KW - CDC
KW - Pore forming toxin
KW - Perforin
KW - Membrane attack complex
KW - Pleurotolysin
UR - http://www.ncbi.nlm.nih.gov/pubmed/26607011
U2 - 10.1016/j.bbamem.2015.11.017
DO - 10.1016/j.bbamem.2015.11.017
M3 - Article
VL - 1858
SP - 475
EP - 486
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
SN - 0005-2736
IS - 3
ER -