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第一作者:GUANGCHAO LIU
第一单位:中科院遗传与发育生物学研究所
通讯作者:FEIFEI YU
Abstarct
背景+问题:Ubiquitination-mediated protein degradation in both the 26S proteasome and vacuole is an important process in abscisic acid (ABA) signaling. However, the role of deubiquitination in this process remains elusive.
在26S蛋白酶体和液泡中,泛素化介导的蛋白降解是脱落酸(ABA)信号转导的一个重要过程。然而,去泛素化在这一过程中的作用仍然不清楚。
主要发现:Here, we demonstrate that two deubiquitinating enzymes (DUBs), ubiquitin-specific protease 12 (UBP12) and UBP13, modulate ABA signaling and drought tolerance by deubiquitinating and stabilizing the endosomal sorting complex required for transport-I (ESCRT-I) component vacuolar protein sorting 23A (VPS23A) and thereby affect the stability of ABA receptors in Arabidopsis thaliana.
本文中,作者发现在拟南芥中,两个去泛素化酶UBP12和UBP13通过去泛素化和稳定内膜分选复合体ESCRT-I组分VPS23A蛋白,进而影响ABA受体的稳定性,最终调控ABA信号转导和干旱耐受性。
结果1-VPS23A恢复UBP12/13突变体表型:Genetic analysis showed that VPS23A overexpression could rescue the ABA hypersensitive and drought tolerance phenotypes of ubp12-2w or ubp13-1.
遗传分析表明,VPS23A过表达可以恢复ubp12-2w或ubp13-1的ABA超敏和耐旱表型。
结果2-UBP12/13-XBAT35.2:In addition to the direct regulation of VPS23A, we found that UBP12 and UBP13 also stabilized the E3 ligase XB3 ortholog 5 in A. thaliana (XBAT35.2) in response to ABA treatment.
除了对VPS23A的直接调控,作者还发现UBP12和UBP13能够响应于ABA的处理,稳定拟南芥中E3连接酶XBAT35.2蛋白。
结论:Hence, we demonstrated that UBP12 and UBP13 are previously unidentified rheostatic regulators of ABA signaling and revealed a mechanism by which deubiquitination precisely monitors the XBAT35/VPS23A ubiquitination module in the ABA response.
因此,本文的研究表明UBP12和UBP13是ABA信号转导的变阻器式调节因子,揭示了一种植物在ABA响应过程中去泛素化精确监测XBAT35/VPS23A泛素化模块的分子机制。
** 于菲菲 **
个人简介: 2005-2009年,曲阜师范大学,学士; 2009-2012年,山东农业大学,硕士; 2012-2016年,中科院遗传与发育生物学研究所,博士; 2017-2021年,中科院遗传与发育生物学研究所,助理研究员、副研究员; 2022年-至今,中国农业大学,教授。 研究方向: 1. 饲草甜高粱耐逆分子机制的解析及饲草品质改良的理论基础研究; 2. 生态治理草及饲草甜高粱分子设计育种; 3. 泛素相关途径参与的非生物逆境分子机制解析。
doi: https://doi.org/10.1126/sciadv.abl5765
Journal: Science Advances
Published date: April 06, 2022
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