Premium
Specific mutations in mammalian P4‐ATPase ATP8A2 catalytic subunit entail differential glycosylation of the accessory CDC50A subunit
Author(s) -
Vestergaard Anna L.,
Mikkelsen Stine A.,
Coleman Jonathan A.,
Molday Robert S.,
Vilsen Bente,
Andersen Jens Peter
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.11.031
Subject(s) - flippase , protein subunit , glycosylation , atpase , biochemistry , microbiology and biotechnology , biology , translocase , chemistry , phospholipid , membrane , phosphatidylserine , enzyme , gene , chromosomal translocation
P4‐ATPases, or flippases, translocate phospholipids between the two leaflets of eukaryotic biological membranes. They are essential to the physiologically crucial phospholipid asymmetry and involved in severe diseases, but their molecular structure and mechanism are still unresolved. Here, we show that in an extensive mutational alanine screening of the mammalian flippase ATP8A2 catalytic subunit, five mutations stand out by leading to reduced glycosylation of the accessory subunit CDC50A. These mutations may disturb the interaction between the subunits.