Ter94 atpase complex targets k11-linked ubiquitinated ci to proteasomes for partial degradation

Zhao Zhang; Xiangdong Lv; Wen chi Yin; Xiaoyun Zhang; Jing Feng; Wenqing Wu; Chi chung Hui; Lei Zhang; Yun Zhao

doi:10.1016/j.devcel.2013.05.006

Ter94 atpase complex targets k11-linked ubiquitinated ci to proteasomes for partial degradation

Zhao Zhang, Xiangdong Lv, Wen chi Yin, Xiaoyun Zhang, Jing Feng, Wenqing Wu, Chi chung Hui, Lei Zhang, Yun Zhao

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

Abstract

The Cubitus interruptus (Ci)/Gli family of transcription factors can be degraded either completely or partially from a full-length form (Ci155/Gli^FL) to a truncated repressor (Ci75/Gli^R) by proteasomes to mediate Hedgehog (Hh) signaling. The mechanism by which proteasomes distinguish ubiquitinated Ci/Gli to carry out complete versus partial degradation is not known. Here, we show that Ter94 ATPase and its mammalian counterpart, p97, are involved in processing Ci and Gli3 into Ci75 and Gli3^R, respectively. Ter94 regulates the partial degradation of ubiquitinated Ci by Cul1-Slimb-based E3 ligase through its adaptors Ufd1-like and dNpl4. Wedemonstrate that Cul1-Slimb-based E3 ligase, but notCul3-Rdx-based E3 ligase, modifies Ci by efficientaddition of K11-linked ubiquitin chains. Ter94^{Ufd1-like/dNpl4} complex interacts directly with Cul1-Slimb, and, intriguingly, it prefers K11-linked ubiquitinated Ci. Thus, Ter94 ATPase and K11-linked ubiquitination in Ci contribute to the selectivity by proteasomes for partial degradation.

Original language	English (US)
Pages (from-to)	636-644
Number of pages	9
Journal	Developmental cell
Volume	25
Issue number	6
DOIs	https://doi.org/10.1016/j.devcel.2013.05.006
State	Published - Jun 24 2013
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology
Developmental Biology
Cell Biology

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10.1016/j.devcel.2013.05.006

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@article{986310f99ad947b3bcfa4126f6642b24,

title = "Ter94 atpase complex targets k11-linked ubiquitinated ci to proteasomes for partial degradation",

abstract = "The Cubitus interruptus (Ci)/Gli family of transcription factors can be degraded either completely or partially from a full-length form (Ci155/GliFL) to a truncated repressor (Ci75/GliR) by proteasomes to mediate Hedgehog (Hh) signaling. The mechanism by which proteasomes distinguish ubiquitinated Ci/Gli to carry out complete versus partial degradation is not known. Here, we show that Ter94 ATPase and its mammalian counterpart, p97, are involved in processing Ci and Gli3 into Ci75 and Gli3R, respectively. Ter94 regulates the partial degradation of ubiquitinated Ci by Cul1-Slimb-based E3 ligase through its adaptors Ufd1-like and dNpl4. Wedemonstrate that Cul1-Slimb-based E3 ligase, but notCul3-Rdx-based E3 ligase, modifies Ci by efficientaddition of K11-linked ubiquitin chains. Ter94Ufd1-like/dNpl4 complex interacts directly with Cul1-Slimb, and, intriguingly, it prefers K11-linked ubiquitinated Ci. Thus, Ter94 ATPase and K11-linked ubiquitination in Ci contribute to the selectivity by proteasomes for partial degradation.",

author = "Zhao Zhang and Xiangdong Lv and Yin, {Wen chi} and Xiaoyun Zhang and Jing Feng and Wenqing Wu and Hui, {Chi chung} and Lei Zhang and Yun Zhao",

note = "Funding Information: We are grateful to Dr. Mary Ann Price for providing Kc167 cells. We thank Drs. Thomas Kornberg, Jin Jiang, Lin Li, Yihong Ye, Cheng-Ting Chien, Baolin Wang, Pao-Tien Chuang, Chao Tong, and Dahua Chen and DSHB, VDRC, NIG, and the Bloomington Stock Center for fly stocks and reagents. We thank Drs. Rong Zeng and Chen Li for helping with mass spectrometry assay. We also thank Drs. Lin Li, Min Wu, Yingzi Yang, Zhengfan Jiang, Zhaocai Zhou, and Jinqiu Zhou for discussions and comments on the manuscript. This work was supported by grants from the National Basic Research Program of China (973 Program: 2011CB943902, 2010CB912101, and 2012CB945001), the National Natural Science Foundation of China (31171414 and 31171394), and the “Strategic Priority Research Program” of the Chinese Academy of Sciences (XDA01010405 and XDA01010406) to Y.Z. and L.Z., as well as grants from the Canadian Cancer Society to C.-c.H. ",

year = "2013",

month = jun,

day = "24",

doi = "10.1016/j.devcel.2013.05.006",

language = "English (US)",

volume = "25",

pages = "636--644",

journal = "Developmental cell",

issn = "1534-5807",

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T1 - Ter94 atpase complex targets k11-linked ubiquitinated ci to proteasomes for partial degradation

AU - Zhang, Zhao

AU - Lv, Xiangdong

AU - Yin, Wen chi

AU - Zhang, Xiaoyun

AU - Feng, Jing

AU - Wu, Wenqing

AU - Hui, Chi chung

AU - Zhang, Lei

AU - Zhao, Yun

N1 - Funding Information: We are grateful to Dr. Mary Ann Price for providing Kc167 cells. We thank Drs. Thomas Kornberg, Jin Jiang, Lin Li, Yihong Ye, Cheng-Ting Chien, Baolin Wang, Pao-Tien Chuang, Chao Tong, and Dahua Chen and DSHB, VDRC, NIG, and the Bloomington Stock Center for fly stocks and reagents. We thank Drs. Rong Zeng and Chen Li for helping with mass spectrometry assay. We also thank Drs. Lin Li, Min Wu, Yingzi Yang, Zhengfan Jiang, Zhaocai Zhou, and Jinqiu Zhou for discussions and comments on the manuscript. This work was supported by grants from the National Basic Research Program of China (973 Program: 2011CB943902, 2010CB912101, and 2012CB945001), the National Natural Science Foundation of China (31171414 and 31171394), and the “Strategic Priority Research Program” of the Chinese Academy of Sciences (XDA01010405 and XDA01010406) to Y.Z. and L.Z., as well as grants from the Canadian Cancer Society to C.-c.H.

PY - 2013/6/24

Y1 - 2013/6/24

N2 - The Cubitus interruptus (Ci)/Gli family of transcription factors can be degraded either completely or partially from a full-length form (Ci155/GliFL) to a truncated repressor (Ci75/GliR) by proteasomes to mediate Hedgehog (Hh) signaling. The mechanism by which proteasomes distinguish ubiquitinated Ci/Gli to carry out complete versus partial degradation is not known. Here, we show that Ter94 ATPase and its mammalian counterpart, p97, are involved in processing Ci and Gli3 into Ci75 and Gli3R, respectively. Ter94 regulates the partial degradation of ubiquitinated Ci by Cul1-Slimb-based E3 ligase through its adaptors Ufd1-like and dNpl4. Wedemonstrate that Cul1-Slimb-based E3 ligase, but notCul3-Rdx-based E3 ligase, modifies Ci by efficientaddition of K11-linked ubiquitin chains. Ter94Ufd1-like/dNpl4 complex interacts directly with Cul1-Slimb, and, intriguingly, it prefers K11-linked ubiquitinated Ci. Thus, Ter94 ATPase and K11-linked ubiquitination in Ci contribute to the selectivity by proteasomes for partial degradation.

AB - The Cubitus interruptus (Ci)/Gli family of transcription factors can be degraded either completely or partially from a full-length form (Ci155/GliFL) to a truncated repressor (Ci75/GliR) by proteasomes to mediate Hedgehog (Hh) signaling. The mechanism by which proteasomes distinguish ubiquitinated Ci/Gli to carry out complete versus partial degradation is not known. Here, we show that Ter94 ATPase and its mammalian counterpart, p97, are involved in processing Ci and Gli3 into Ci75 and Gli3R, respectively. Ter94 regulates the partial degradation of ubiquitinated Ci by Cul1-Slimb-based E3 ligase through its adaptors Ufd1-like and dNpl4. Wedemonstrate that Cul1-Slimb-based E3 ligase, but notCul3-Rdx-based E3 ligase, modifies Ci by efficientaddition of K11-linked ubiquitin chains. Ter94Ufd1-like/dNpl4 complex interacts directly with Cul1-Slimb, and, intriguingly, it prefers K11-linked ubiquitinated Ci. Thus, Ter94 ATPase and K11-linked ubiquitination in Ci contribute to the selectivity by proteasomes for partial degradation.

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DO - 10.1016/j.devcel.2013.05.006

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JF - Developmental cell

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ER -

Ter94 atpase complex targets k11-linked ubiquitinated ci to proteasomes for partial degradation

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