Rattlesnake Phospholipase A2 Increases CFTR-Chloride Channel Current and Corrects ∆ F508CFTR Dysfunction: Impact in Cystic Fibrosis
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- 作者：Grazyna Faure1 ; &dagger ; ; grazyna.faure-kuzminska@pasteur.fr" class="auth_mail" title="E-mail the corresponding author ; Naziha Bakouh2 ; &Dagger ; ; Sté ; phane Lourdel3 ; &Dagger ; ; Norbert Odolczyk4 ; &Dagger ; ; Aiswarya Premchandar4 ; &Dagger ; ; Nathalie Servel2 ; Auré ; lie Hatton2 ; Maciej K. Ostrowski1 ; Haijin Xu1 ; Frederick A. Saul5 ; Christelle Moquereau2 ; Sara Bitam2 ; Iwona Pranke2 ; Gabrielle Planelles2 ; Jacques Teulon3 ; Harald Herrmann6 ; 8 ; Ariel Roldan7 ; Piotr Zielenkiewicz4 ; Michal Dadlez4 ; Gergely L. Lukacs7 ; Isabelle Sermet-Gaudelus2 ; Mario Ollero2 ; 9 ; Pierre-Jean Corringer1 ; Aleksander Edelman2 ; &dagger ;
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：17 July 2016
- 年：2016
- 卷：428
- 期：14
- 页码：2898-2915
- 全文大小：1718 K
文摘
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The CB subunit of crotoxin is a novel binding partner for CFTR.
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CB binding to CFTR potentiates chloride channel current in normal and ∆ F508CFTR.
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CB interaction with ∆ F508CFTR corrects its cellular localization defect.
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A structural model of the CB/ΔF508CFTR binding interface is presented.
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CB–CFTR interaction constitutes a novel target of therapeutic strategies in CF.
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