ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Feifei Yu; Lijuan Lou; Miaomiao Tian; Qingliang Li; Yanglin Ding; Xiaoqiang Cao; Yaorong Wu; Borja Belda-Palazon; Pedro L Rodriguez; Shuhua Yang; Qi Xie

doi:10.1016/j.molp.2016.11.002

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Mol Plant. 2016 Dec 5;9(12):1570-1582. doi: 10.1016/j.molp.2016.11.002. Epub 2016 Nov 14.

Authors

Affiliations

¹ State Key Laboratory of Plant Genomics, National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Chaoyang District, Beijing 100101, P. R. China; College of Life Science, University of Chinese Academy of Sciences, Beijing 100049, P. R. China.
² State Key Laboratory of Plant Genomics, National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Chaoyang District, Beijing 100101, P. R. China.
³ State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
⁴ Instituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, 46022 Valencia, Spain.
⁵ State Key Laboratory of Plant Genomics, National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Chaoyang District, Beijing 100101, P. R. China. Electronic address: qxie@genetics.ac.cn.

PMID: 27856401
DOI: 10.1016/j.molp.2016.11.002

Abstract

Recent discovery of PYR/PYL/RCAR-type abscisic acid (ABA) receptors has become one of most significant advances in plant science in the past decade. In mammals, endosomal sorting acts as an important pathway to downregulate different types of receptors, but its role in plant hormone signaling is poorly understood. Here, we report that an ubiquitin E2-like protein, VPS23A, which is a key component of ESCRT-I, negatively regulates ABA signaling. VPS23A has epistatic relationship with PYR/PYL/RCAR-type ABA receptors and disruption of VPS23A enhanced the activity of key kinase OST1 in the ABA signaling pathway under ABA treatment. Moreover, VPS23A interacts with PYR1/PYLs and K63-linked diubiquitin, and PYL4 possesses K63-linked ubiquitinated modification in vivo. Further analysis revealed that VPS23A affects the subcellular localization of PYR1 and the stability of PYL4. Taken together, our results suggest that VPS23A affects PYR1/PYL4 via vacuole-mediated degradation, providing an advanced understanding of both the turnover of ABA receptors and ESCRTs in plant hormone signaling.

Keywords: ABA receptors; ESCRTs; endosomal trafficking; ubiquitin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Abscisic Acid / pharmacology*
Arabidopsis / drug effects*
Arabidopsis / genetics
Arabidopsis / metabolism*
Arabidopsis Proteins / genetics
Arabidopsis Proteins / metabolism*
Endosomal Sorting Complexes Required for Transport / genetics
Endosomal Sorting Complexes Required for Transport / metabolism
Gene Expression Regulation, Plant
Plant Growth Regulators / pharmacology*
Protein Binding / drug effects
Protein Binding / genetics
Receptors, Cell Surface / genetics
Receptors, Cell Surface / metabolism
Signal Transduction / drug effects
Signal Transduction / genetics

Substances

Arabidopsis Proteins
Endosomal Sorting Complexes Required for Transport
Plant Growth Regulators
Receptors, Cell Surface
Abscisic Acid