Membrane-integration Characteristics of Two ABC Transporters, CFTR and P-glycoprotein |
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Authors: | Karl Enquist Mawritz Fransson Carolina Boekel Inger Bengtsson Lisa Lang Sofia Johansson IngMarie Nilsson |
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Affiliation: | 1 Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden 2 Stockholm Bioinformatics Center, AlbaNova, SE-106 91 Stockholm, Sweden |
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Abstract: | To what extent do corresponding transmembrane helices in related integral membrane proteins have different membrane-insertion characteristics? Here, we compare, side-by-side, the membrane insertion characteristics of the 12 transmembrane helices in the adenosine triphosphate-binding cassette (ABC) transporters, P-glycoprotein (P-gp) and the cystic fibrosis transmembrane conductance regulator (CFTR). Our results show that 10 of the 12 CFTR transmembrane segments can insert independently into the ER membrane. In contrast, only three of the P-gp transmembrane segments are independently stable in the membrane, while the majority depend on the presence of neighboring loops and/or transmembrane segments for efficient insertion. Membrane-insertion characteristics can thus vary widely between related proteins. |
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Keywords: | CF, cystic fibrosis CFTR, cystic fibrosis transmembrane conductance regulator P-gp, P-glycoprotein TM, transmembrane ABC transporter, ATP-binding cassette transporter ER, endoplasmic reticulum CRM, column-washed dog pancreas rough microsomes Lep, leader peptidase |
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