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ESCRT-I Component VPS23A Is Targeted by E3 Ubiquitin Ligase XBAT35 for Proteasome-Mediated Degradation in Modulating ABA Signaling
Feifei Yu, Xiaoqiang Cao, Guangchao Liu, Qian Wang, Ran Xia, Xiangyun Zhang, Qi Xie
Molecular Plant
Abstract
Myriad abiotic stress responses in plants are controlled by abscisic acid (ABA) signaling, and ABA receptor proteins are recently studied to be degraded by the 26S proteasome pathway and by vacuolar degradation after processing via endosomal sorting complex required for transport (ESCRT) proteins. Despite their known essentiality in ABA signaling, the upstream regulators of ESCRTs remain unknown. Here, we report that the ESCRT-I component VPS23A is an unstable protein that is degraded via the ubiquitin-proteasome system. The UEV domain of VPS23A physically interacts with the two PSAP motifs of XBAT35, and this interaction results in the deposition of K48 polyubiquitin chains on VPS23A, thusly targeting it for degradation via 26S proteasomes. We show that XBAT35 in plants is a positive regulator of responses to ABA that acts via the VPS23A/PYL4 complex, specifically by accelerating VPS23A turnover, thereby increasing accumulation of the ABA receptor PYL4. Thus, beyond offering the first demonstration of how an ESCRT component is regulated in plants, this study deepens our understanding of plant stress responses by illustrating a mechanism wherein crosstalk between the ubiquitin-proteasome system (UPS) and endosome-vacuole mediated degradation pathways controls ABA signaling.
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论文编号: |
DOI:10.1016/j.molp.2020.09.008 |
论文题目: |
ESCRT-I Component VPS23A Is Targeted by E3 Ubiquitin Ligase XBAT35 for Proteasome-Mediated Degradation in Modulating ABA Signaling |
英文论文题目: |
ESCRT-I Component VPS23A Is Targeted by E3 Ubiquitin Ligase XBAT35 for Proteasome-Mediated Degradation in Modulating ABA Signaling |
第一作者: |
Feifei Yu, Xiaoqiang Cao, Guangchao Liu, Qian Wang, Ran Xia, Xiangyun Zhang, Qi Xie |
英文第一作者: |
Feifei Yu, Xiaoqiang Cao, Guangchao Liu, Qian Wang, Ran Xia, Xiangyun Zhang, Qi Xie |
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2020-09-13 |
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摘要: |
Myriad abiotic stress responses in plants are controlled by abscisic acid (ABA) signaling, and ABA receptor proteins are recently studied to be degraded by the 26S proteasome pathway and by vacuolar degradation after processing via endosomal sorting complex required for transport (ESCRT) proteins. Despite their known essentiality in ABA signaling, the upstream regulators of ESCRTs remain unknown. Here, we report that the ESCRT-I component VPS23A is an unstable protein that is degraded via the ubiquitin-proteasome system. The UEV domain of VPS23A physically interacts with the two PSAP motifs of XBAT35, and this interaction results in the deposition of K48 polyubiquitin chains on VPS23A, thusly targeting it for degradation via 26S proteasomes. We show that XBAT35 in plants is a positive regulator of responses to ABA that acts via the VPS23A/PYL4 complex, specifically by accelerating VPS23A turnover, thereby increasing accumulation of the ABA receptor PYL4. Thus, beyond offering the first demonstration of how an ESCRT component is regulated in plants, this study deepens our understanding of plant stress responses by illustrating a mechanism wherein crosstalk between the ubiquitin-proteasome system (UPS) and endosome-vacuole mediated degradation pathways controls ABA signaling. |
英文摘要: |
Myriad abiotic stress responses in plants are controlled by abscisic acid (ABA) signaling, and ABA receptor proteins are recently studied to be degraded by the 26S proteasome pathway and by vacuolar degradation after processing via endosomal sorting complex required for transport (ESCRT) proteins. Despite their known essentiality in ABA signaling, the upstream regulators of ESCRTs remain unknown. Here, we report that the ESCRT-I component VPS23A is an unstable protein that is degraded via the ubiquitin-proteasome system. The UEV domain of VPS23A physically interacts with the two PSAP motifs of XBAT35, and this interaction results in the deposition of K48 polyubiquitin chains on VPS23A, thusly targeting it for degradation via 26S proteasomes. We show that XBAT35 in plants is a positive regulator of responses to ABA that acts via the VPS23A/PYL4 complex, specifically by accelerating VPS23A turnover, thereby increasing accumulation of the ABA receptor PYL4. Thus, beyond offering the first demonstration of how an ESCRT component is regulated in plants, this study deepens our understanding of plant stress responses by illustrating a mechanism wherein crosstalk between the ubiquitin-proteasome system (UPS) and endosome-vacuole mediated degradation pathways controls ABA signaling. |
刊物名称: |
Molecular Plant |
英文刊物名称: |
Molecular Plant |
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其它备注: |
Feifei Yu, Xiaoqiang Cao, Guangchao Liu, Qian Wang, Ran Xia, Xiangyun Zhang, Qi Xie. ESCRT-I Component VPS23A Is Targeted by E3 Ubiquitin Ligase XBAT35 for Proteasome-Mediated Degradation in Modulating ABA Signaling. Molecular Plant. DOI:10.1016/j.molp.2020.09.008 |
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