Release date: 2018-01-04
The research results of the Zhao Yun Research Group of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, published on the EMBO Reports online under the title UbcD1 regulates Hedgehog signaling by directly modulating Ci ubiquitination and processing. This study found that UbcD1 regulates the protein stability of the key transcription factor Ci/Gli in the Hh signaling pathway.
The Hh signaling pathway plays an important role in embryonic development, maintenance of adult tissue homeostasis, and tumor development. Abnormalities in the Hh signaling pathway can trigger a variety of serious human diseases, including some birth defects and cancer. The activity of the transcription factor Ci/Gli is strictly regulated by a variety of post-translational modifications. The ubiquitination-mediated proteasome degradation directly regulates the stability and protein level of Ci/Gli, and therefore is important for the activity level of Hh signaling pathway. Regulation. There are two important ubiquitination regulation methods in the Hh signaling pathway. When there is no Hh signal, Ci/Gli ubiquitination is mediated by Slimb-Cul1 E3 ligase to cause selective partial degradation; when high concentration of Hh signal is present, Ci/Gli ubiquitination is mediated by Rdx-Cul3 E3 ligase Further complete degradation occurs. In the preliminary study of Zhao Yun's research group, the Ter94 ATPase complex, the lysine K11 ubiquitin chain of UB and the Sqh molecule are important for mediating the selective partial degradation of Ci/Gli during the selective degradation of Ci/Gli. At the same time, the ubiquitination enzyme Usp7 participates in the regulation of the stability of Ci/Gli by regulating the level of ubiquitination. However, it is unknown whether the ubiquitin-conjugating enzyme is specific for the selective degradation of Ci/Gli and whether it plays a role in determining the ubiquitin chain species.
In the study, Dr. Pan Chenyu of Zhao Yun's research group found that E2--UbcD1 regulates the protein stability of Ci/Gli by genetic screening and specifically participates in the Slimb-Cul1 E3 ligase-mediated Ci ubiquitination degradation process. Rdx-Cul3 E3 ligase-mediated ubiquitination of Ci/Gli does not work. UbcD1 is also involved in the formation of K-11 ubiquitin chains during the ubiquitination degradation of Ci/Gli. At the same time, this regulatory mechanism is highly conserved in vertebrates. This work further revealed the stable regulation mechanism of the Hh pathway transcription factor Ci/Gli and also provided a potential drug target for the regulation of Ci/Gli degradation.
The research was supported by the biochemical and cellular cell analysis technology platform, the fruit fly resource and technology platform, the zebrafish technology platform and the molecular biology technology platform, and was awarded the Ministry of Science and Technology, the National Natural Science Foundation of China, the Chinese Academy of Sciences and Shanghai. City funding.
Source: Shanghai Academy of Health Sciences
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