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Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms
Pore-forming proteins play critical roles in pathogenic attack and immunological defence. The membrane attack complex/perforin (MACPF) group of homologues represents, with cholesterol-dependent cytolysins, the largest family of such proteins. In this review, we begin by describing briefly the struct...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5483515/ https://www.ncbi.nlm.nih.gov/pubmed/28630152 http://dx.doi.org/10.1098/rstb.2016.0212 |
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author | Ni, Tao Gilbert, Robert J. C. |
author_facet | Ni, Tao Gilbert, Robert J. C. |
author_sort | Ni, Tao |
collection | PubMed |
description | Pore-forming proteins play critical roles in pathogenic attack and immunological defence. The membrane attack complex/perforin (MACPF) group of homologues represents, with cholesterol-dependent cytolysins, the largest family of such proteins. In this review, we begin by describing briefly the structure of MACPF proteins, outlining their common mechanism of pore formation. We subsequently discuss some examples of MACPF proteins likely implicated in pore formation or other membrane-remodelling processes. Finally, we focus on astrotactin and bone morphogenetic protein and retinoic acid-induced neural-specific proteins, highly conserved MACPF family members involved in developmental processes, which have not been well studied to date or observed to form a pore—and which data suggest may act by alternative mechanisms. This article is part of the themed issue ‘Membrane pores: from structure and assembly, to medicine and technology’. |
format | Online Article Text |
id | pubmed-5483515 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-54835152017-06-26 Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms Ni, Tao Gilbert, Robert J. C. Philos Trans R Soc Lond B Biol Sci Articles Pore-forming proteins play critical roles in pathogenic attack and immunological defence. The membrane attack complex/perforin (MACPF) group of homologues represents, with cholesterol-dependent cytolysins, the largest family of such proteins. In this review, we begin by describing briefly the structure of MACPF proteins, outlining their common mechanism of pore formation. We subsequently discuss some examples of MACPF proteins likely implicated in pore formation or other membrane-remodelling processes. Finally, we focus on astrotactin and bone morphogenetic protein and retinoic acid-induced neural-specific proteins, highly conserved MACPF family members involved in developmental processes, which have not been well studied to date or observed to form a pore—and which data suggest may act by alternative mechanisms. This article is part of the themed issue ‘Membrane pores: from structure and assembly, to medicine and technology’. The Royal Society 2017-08-05 2017-06-19 /pmc/articles/PMC5483515/ /pubmed/28630152 http://dx.doi.org/10.1098/rstb.2016.0212 Text en © 2017 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Articles Ni, Tao Gilbert, Robert J. C. Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |
title | Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |
title_full | Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |
title_fullStr | Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |
title_full_unstemmed | Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |
title_short | Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |
title_sort | repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5483515/ https://www.ncbi.nlm.nih.gov/pubmed/28630152 http://dx.doi.org/10.1098/rstb.2016.0212 |
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