J 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.