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

[EN] 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 i...

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Detalles Bibliográficos
Autores: Yu, Feifei, Lou, Lijuan, Tian, Miaomiao, Li, Qingliang, Ding, Yanglin, Cao, Xiaoqiang, Wu, Yaorong, Yang, Shuhua, Xie, Qi, Belda Palazón, Borja, Rodríguez Egea, Pedro Luís|||0000-0002-5886-9425
Tipo de recurso: artículo
Fecha de publicación:2016
País:España
Institución:Universitat Politècnica de València (UPV)
Repositorio:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
Idioma:inglés
OAI Identifier:oai:riunet.upv.es:10251/82419
Acceso en línea:https://riunet.upv.es/handle/10251/82419
Access Level:acceso abierto
Palabra clave:ABA receptors
ESCRTs
Ubiquitin
Endosomal trafficking
BIOQUIMICA Y BIOLOGIA MOLECULAR
Descripción
Sumario:[EN] 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.

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