Detailed Information on Publication Record
2023
An LRR receptor kinase controls ABC transporter substrate preferences during plant growth-defense decisions
ARYAL, Bibek, Jian XIA, Zehan HU, Michael STUMPE, Tashi TSERING et. al.Basic information
Original name
An LRR receptor kinase controls ABC transporter substrate preferences during plant growth-defense decisions
Authors
ARYAL, Bibek, Jian XIA, Zehan HU, Michael STUMPE, Tashi TSERING, Jie LIU, John HUYNH, Yoichiro FUKAO, Nina GLOECKNER, Hsin -Yao HUANG, Gloria SANCHO-ANDRES, Konrad PAKULA, Joerg ZIEGLER, Karin GORZOLKA, Marta ZWIEWKA (616 Poland, belonging to the institution), Tomasz NODZYNSKI (616 Poland, belonging to the institution), Klaus HARTER, Clara SANCHEZ-RODRIGUEZ, Michal JASINSKI, Sabine ROSAHL and Markus M GEISLER (guarantor)
Edition
Current Biology, CAMBRIDGE, CELL PRESS, 2023, 0960-9822
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 9.200 in 2022
RIV identification code
RIV/00216224:14740/23:00133147
Organization unit
Central European Institute of Technology
UT WoS
001011980000001
Keywords in English
plasma membrane proteins; auxin transport; necrotrophic pathogens; arabidopsis thaliana; phosphoproteomics
Tags
Tags
International impact, Reviewed
Změněno: 25/2/2024 22:01, Mgr. Eva Dubská
Abstract
V originále
The exporter of the auxin precursor indole-3-butyric acid (IBA), ABCG36/PDR8/PEN3, from the model plant Arabidopsis has recently been proposed to also function in the transport of the phytoalexin camalexin. Based on these bonafide substrates, it has been suggested that ABCG36 functions at the interface between growth and defense. Here, we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the plasma membrane. We identify the leucine-rich repeat receptor kinase, QIAN SHOU KINASE1 (QSK1), as a functional kinase that physically interacts with and phosphorylates ABCG36. Phosphorylation of ABCG36 by QSK1 unilaterally represses IBA export, allowing camalexin export by ABCG36 conferring pathogen resis-tance. As a consequence, phospho-dead mutants of ABCG36, as well as qsk1 and abcg36 alleles, are hyper-sensitive to infection with the root pathogen Fusarium oxysporum, caused by elevated fungal progression. Our findings indicate a direct regulatory circuit between a receptor kinase and an ABC transporter that func-tions to control transporter substrate preference during plant growth and defense balance decisions.