Role of post-translational modifications at the β-subunit ectodomain in complex association with a promiscuous plant P4-ATPase.

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Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Role of post-translational modifications at the β-subunit ectodomain in complex association with a promiscuous plant P4-ATPase.
Journal
Biochemical Journal
Author(s)
Costa S.R., Marek M., Axelsen K.B., Theorin L., Pomorski T.G., López-Marqués R.L.
ISSN
1470-8728 (Electronic)
ISSN-L
0264-6021
Publication state
Published
Issued date
2016
Peer-reviewed
Oui
Volume
473
Number
11
Pages
1605-1615
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
P-type ATPases of subfamily IV (P4-ATPases) constitute a major group of phospholipid flippases that form heteromeric complexes with members of the Cdc50 (cell division control 50) protein family. Some P4-ATPases interact specifically with only one β-subunit isoform, whereas others are promiscuous and can interact with several isoforms. In the present study, we used a site-directed mutagenesis approach to assess the role of post-translational modifications at the plant ALIS5 β-subunit ectodomain in the functionality of the promiscuous plant P4-ATPase ALA2. We identified two N-glycosylated residues, Asn(181) and Asn(231) Whereas mutation of Asn(231) seems to have a small effect on P4-ATPase complex formation, mutation of evolutionarily conserved Asn(181) disrupts interaction between the two subunits. Of the four cysteine residues located in the ALIS5 ectodomain, mutation of Cys(86) and Cys(107) compromises complex association, but the mutant β-subunits still promote complex trafficking and activity to some extent. In contrast, disruption of a conserved disulfide bond between Cys(158) and Cys(172) has no effect on the P4-ATPase complex. Our results demonstrate that post-translational modifications in the β-subunit have different functional roles in different organisms, which may be related to the promiscuity of the P4-ATPase.
Keywords
Arabidopsis thaliana, Cdc50 ectodomain, disulfide bond, flippase, N-glycosylation
Pubmed
Web of science
Create date
14/04/2016 16:26
Last modification date
20/08/2019 14:39
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