Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding
Export of Plasmodium falciparum proteins into infected erythrocytes relies upon the PEXEL motif in target proteins. Here Boddey et al.challenge the hypothesis that the PEXEL motif mediates export by binding PI(3)P and instead suggest it acts via cleavage by plasmepsin V.
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Nature Portfolio
2016
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oai:doaj.org-article:9c31a074ac774adfad666d242b4d3b612021-12-02T15:33:49ZExport of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding10.1038/ncomms104702041-1723https://doaj.org/article/9c31a074ac774adfad666d242b4d3b612016-02-01T00:00:00Zhttps://doi.org/10.1038/ncomms10470https://doaj.org/toc/2041-1723Export of Plasmodium falciparum proteins into infected erythrocytes relies upon the PEXEL motif in target proteins. Here Boddey et al.challenge the hypothesis that the PEXEL motif mediates export by binding PI(3)P and instead suggest it acts via cleavage by plasmepsin V.Justin A. BoddeyMatthew T. O’NeillSash LopatickiTeresa G. CarvalhoAnthony N. HodderThomas NeblStephan WawraPieter van WestZeinab EbrahimzadehDave RichardSven FlemmingTobias SpielmannJude PrzyborskiJeff J. BabonAlan F. CowmanNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-14 (2016) |
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spellingShingle |
Science Q Justin A. Boddey Matthew T. O’Neill Sash Lopaticki Teresa G. Carvalho Anthony N. Hodder Thomas Nebl Stephan Wawra Pieter van West Zeinab Ebrahimzadeh Dave Richard Sven Flemming Tobias Spielmann Jude Przyborski Jeff J. Babon Alan F. Cowman Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding |
description |
Export of Plasmodium falciparum proteins into infected erythrocytes relies upon the PEXEL motif in target proteins. Here Boddey et al.challenge the hypothesis that the PEXEL motif mediates export by binding PI(3)P and instead suggest it acts via cleavage by plasmepsin V. |
format |
article |
author |
Justin A. Boddey Matthew T. O’Neill Sash Lopaticki Teresa G. Carvalho Anthony N. Hodder Thomas Nebl Stephan Wawra Pieter van West Zeinab Ebrahimzadeh Dave Richard Sven Flemming Tobias Spielmann Jude Przyborski Jeff J. Babon Alan F. Cowman |
author_facet |
Justin A. Boddey Matthew T. O’Neill Sash Lopaticki Teresa G. Carvalho Anthony N. Hodder Thomas Nebl Stephan Wawra Pieter van West Zeinab Ebrahimzadeh Dave Richard Sven Flemming Tobias Spielmann Jude Przyborski Jeff J. Babon Alan F. Cowman |
author_sort |
Justin A. Boddey |
title |
Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding |
title_short |
Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding |
title_full |
Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding |
title_fullStr |
Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding |
title_full_unstemmed |
Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding |
title_sort |
export of malaria proteins requires co-translational processing of the pexel motif independent of phosphatidylinositol-3-phosphate binding |
publisher |
Nature Portfolio |
publishDate |
2016 |
url |
https://doaj.org/article/9c31a074ac774adfad666d242b4d3b61 |
work_keys_str_mv |
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1718387040249184256 |