Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8383988 | FEBS Letters | 2015 | 8 Pages |
Abstract
The function of the ATP-binding cassette transporter MRP6 is unknown but mutations in its gene cause pseudoxanthoma elasticum. We have investigated the membrane topology of the N-terminal transmembrane domain TMD0 of MRP6 and the membrane integration and orientation propensities of its transmembrane segments (TMs) by glycosylation mapping. Results demonstrate that TMD0 has five TMs, an Nout-Cin topology and that the less hydrophobic TMs have strong preference for their orientation in the membrane that affects the neighboring TMs. Two disease-causing mutations changing the number of positive charges in the loops of TMD0 did not affect the membrane insertion efficiencies of the adjacent TMs.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Flavia Cuviello, Ã
sa Tellgren-Roth, Patricia Lara, Frida Ruud Selin, Magnus Monné, Faustino Bisaccia, IngMarie Nilsson, Angela Ostuni,