SERK Family Receptor-like Kinases Function as Co-receptors with PXY for Plant Vascular Development

In Arabidopsis, the CLAVATA3/EMBRYO SURROUNDING REGION-RELATED （CLE） peptides play important roles in regulating proliferation and differentiation of plant-specific stem cells. Although receptors of CLEs are reported to be leucine-rich repeat receptor kinases, the mechanisms underlying CLE-induced r...

Full description

Saved in:
Bibliographic Details
Published in:Molecular plant 2016-10, Vol.9 (10), p.1406-1414
Main Authors: Zhang, Heqiao, Lin, Xiaoya, Han, Zhifu, Wang, Jizong, Qu, Li-Jia, Chai, Jijie
Format: Article
Language:English
Subjects:
Arabidopsis - genetics
Arabidopsis - growth & development
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Cell Proliferation - genetics
Cell Proliferation - physiology
co-receptor
Gene Expression Regulation, Plant
Oligopeptides - genetics
Oligopeptides - metabolism
Protein Kinases - genetics
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
PXY-TDIF
receptor-like kinase
SERK
vascular development
Xylem - growth & development
Xylem - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In Arabidopsis, the CLAVATA3/EMBRYO SURROUNDING REGION-RELATED （CLE） peptides play important roles in regulating proliferation and differentiation of plant-specific stem cells. Although receptors of CLEs are reported to be leucine-rich repeat receptor kinases, the mechanisms underlying CLE-induced receptor activation remain largely unknown. Here we show that SOMATIC EMBRYOGENESIS RECEPTOR KINASEs （SERKs） serve as co-receptors in CLE41/TDIF-PXY signaling to regulate plant vascular development. TDIF induces interaction of its receptor PXY with SERKs in vitro and in vivo. Furthermore, the serk1-1 serk2-1 bakl-5 mutant plants are less sensitive to TDIF, phenocopying the pxy mutant with a compromised promotion of procambial cell proliferation. Crystal structure of the PXY-TDIF-SERK2 complex reveals that the last amino acid of TDIF conserved among CLEs and other evolutionary-related peptides is important for the interaction between SERK2 and PXY. Taken together, our current study identifies SERKs as signaling components of the TDIF-PXY pathway and suggests a conserved activation mechanism of CLE receptors.
ISSN:1674-2052
1752-9867
DOI:10.1016/j.molp.2016.07.004