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Membrane insertion and topology of the amino-terminal domain TMD0 of multidrug-resistance associated protein 6 (MRP6)
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Vise andre og tillknytning
2015 (engelsk)Inngår i: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 589, nr 24, s. 3921-3928Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
2015. Vol. 589, nr 24, s. 3921-3928
Emneord [en]
ATP-binding cassette transporter, Multidrug-resistance associated protein 6, ABCC6, Transmembrane domain, Pseudoxanthoma elasticum, Membrane protein insertion
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Identifikatorer
URN: urn:nbn:se:su:diva-124228DOI: 10.1016/j.febslet.2015.10.030ISI: 000367232900019PubMedID: 26545497OAI: oai:DiVA.org:su-124228DiVA, id: diva2:882804
Tilgjengelig fra: 2015-12-15 Laget: 2015-12-15 Sist oppdatert: 2022-02-23bibliografisk kontrollert

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Tellgren-Roth, ÅsaLara, PatriciaNilsson, IngMarie

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