Mapping and engineering of auxin-induced plasma membrane dissociation in BRX family proteins.

Details

Serval ID
serval:BIB_157F3074C32D
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Mapping and engineering of auxin-induced plasma membrane dissociation in BRX family proteins.
Journal
The Plant cell
Author(s)
Koh SWH, Marhava P., Rana S., Graf A., Moret B., Bassukas AEL, Zourelidou M., Kolb M., Hammes U.Z., Schwechheimer C., Hardtke C.S.
ISSN
1532-298X (Electronic)
ISSN-L
1040-4651
Publication state
Published
Issued date
19/07/2021
Peer-reviewed
Oui
Volume
33
Number
6
Pages
1945-1960
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
Angiosperms have evolved the phloem for the long-distance transport of metabolites. The complex process of phloem development involves genes that only occur in vascular plant lineages. For example, in Arabidopsis thaliana, the BREVIS RADIX (BRX) gene is required for continuous root protophloem differentiation, together with PROTEIN KINASE ASSOCIATED WITH BRX (PAX). BRX and its BRX-LIKE (BRXL) homologs are composed of four highly conserved domains including the signature tandem BRX domains that are separated by variable spacers. Nevertheless, BRX family proteins have functionally diverged. For instance, BRXL2 can only partially replace BRX in the root protophloem. This divergence is reflected in physiologically relevant differences in protein behavior, such as auxin-induced plasma membrane dissociation of BRX, which is not observed for BRXL2. Here we dissected the differential functions of BRX family proteins using a set of amino acid substitutions and domain swaps. Our data suggest that the plasma membrane-associated tandem BRX domains are both necessary and sufficient to convey the biological outputs of BRX function and therefore constitute an important regulatory entity. Moreover, PAX target phosphosites in the linker between the two BRX domains mediate the auxin-induced plasma membrane dissociation. Engineering these sites into BRXL2 renders this modified protein auxin-responsive and thereby increases its biological activity in the root protophloem context.
Keywords
Plant Science, Cell Biology
Pubmed
Open Access
Yes
Create date
29/03/2021 12:00
Last modification date
27/07/2021 6:36
Usage data