Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 윤채옥 | - |
dc.date.accessioned | 2019-12-04T01:19:20Z | - |
dc.date.available | 2019-12-04T01:19:20Z | - |
dc.date.issued | 2018-01 | - |
dc.identifier.citation | CELL DEATH & DISEASE, v. 9, Article no. 97 | en_US |
dc.identifier.issn | 2041-4889 | - |
dc.identifier.uri | https://www.nature.com/articles/s41419-017-0138-9 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/116984 | - |
dc.description.abstract | The carboxyl terminus of Hsp70-interacting protein (CHIP) acts as a ubiquitin E3 ligase and a link between the chaperones Hsp70/90 and the proteasome system, playing a vital role in maintaining protein homeostasis. CHIP regulates a number of proteins involved in a myriad of physiological and pathological processes, but the underlying mechanism of action via posttranslational modification has not been extensively explored. In this study, we investigated a novel modulatory mode of CHIP and its effect on CHIP enzymatic activity. ISG15, an ubiquitin-like modifier, is induced by type I interferon (IFN) stimulation and can be conjugated to target proteins (ISGylation). Here we demonstrated that CHIP may be a novel target of ISGylation in HEK293 cells stimulated with type I IFN. We also found that Lys143/144/145 and Lys287 residues in CHIP are important for and target residues of ISGylation. Moreover, ISGylation promotes the E3 ubiquitin ligase activity of CHIP, subsequently causing a decrease in levels of oncogenic c-Myc, one of its many ubiquitination targets, in A549 lung cancer cells and inhibiting A549 cell and tumor growth. In conclusion, the present study demonstrates that covalent ISG15 conjugation produces a novel CHIP regulatory mode that enhances the tumor-suppressive activity of CHIP, thereby contributing to the antitumor effect of type I IFN. | en_US |
dc.description.sponsorship | This work was supported by grants from the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT & Future Planning (2014M3C7A1064545 to K.C.C.) and from the Korea Healthcare Technology R&D Project through the Korea Health Industry Development Institute (KHIDI) funded by the Ministry of Health & Welfare (HI17C0936 to K.C.C.), Republic of Korea. This work was also supported in part by the NRF grant (2015R1A2A2A01003080 to K.C.C.) and by the Yonsei University Future-leading Research Initiative of 2015 (2015-22-0055 to K.C.C.). | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | NATURE PUBLISHING GROUP | en_US |
dc.subject | HSC70-INTERACTING PROTEIN CHIP | en_US |
dc.subject | C-MYC EXPRESSION | en_US |
dc.subject | MEDIATED DEGRADATION | en_US |
dc.subject | IDENTIFICATION | en_US |
dc.subject | ARREST | en_US |
dc.subject | ACTIVATION | en_US |
dc.subject | APOPTOSIS | en_US |
dc.subject | CYTOKINE | en_US |
dc.subject | TERMINUS | en_US |
dc.subject | TARGET | en_US |
dc.title | Covalent ISG15 conjugation to CHIP promotes its ubiquitin E3 ligase activity and inhibits lung cancer cell growth in response to type I interferon | en_US |
dc.type | Article | en_US |
dc.relation.volume | 9 | - |
dc.identifier.doi | 10.1038/s41419-017-0138-9 | - |
dc.relation.page | 1-10 | - |
dc.relation.journal | CELL DEATH & DISEASE | - |
dc.contributor.googleauthor | Yoo, Lang | - |
dc.contributor.googleauthor | Yoon, A-Rum | - |
dc.contributor.googleauthor | Yun, Chae-Ok | - |
dc.contributor.googleauthor | Chung, Kwang Chul | - |
dc.relation.code | 2018012490 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF ENGINEERING[S] | - |
dc.sector.department | DEPARTMENT OF BIOENGINEERING | - |
dc.identifier.pid | chaeok | - |
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