1. USP21 modulates Goosecoid function through deubiquitination
- Author
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Kai Zhang, Liang Kong, Mingyue Tang, Qian Fu, Wei Jiang, Bin Bo, Yajun Cui, Liu Fuwei, and Li Yunpeng
- Subjects
0301 basic medicine ,endocrine system ,animal structures ,Biophysics ,Goosecoid ,USP21 ,Transfection ,Biochemistry ,law.invention ,03 medical and health sciences ,0302 clinical medicine ,Ubiquitin ,Transcription (biology) ,law ,Humans ,Viability assay ,Amino Acid Sequence ,Molecular Biology ,Research Articles ,Reporter gene ,biology ,Deubiquitinating Enzymes ,fungi ,Sox6 reporter gene system ,Genes, Homeobox ,Ubiquitination ,Cell Biology ,Cell biology ,Repressor Proteins ,Goosecoid Protein ,030104 developmental biology ,Testis determining factor ,HEK293 Cells ,030220 oncology & carcinogenesis ,embryonic structures ,Proteolysis ,Recombinant DNA ,biology.protein ,Homeobox ,Deubiquitination ,SOXD Transcription Factors ,Ubiquitin Thiolesterase ,Research Article - Abstract
The homeobox gene Goosecoid (GSC), which is known to regulate craniofacial development, is activated by mono-ubiquitination; however, the deubiquitylase responsible for GSC deubiquitination and inhibition has yet to be identified. In the present study, we constructed the recombinant plasmid pFlag-CMV-2-GSC and the SRY (sex-determining region Y)-box 6 (Sox6) reporter gene system to identify deubiquitylases that regulate GSC expression. We demonstrate that the ubiquitin carboxyl-terminal hydrolase 21 (USP21) regulates the deubiquitination of GSC negatively, as demonstrated by its inhibition of Sox6 reporter gene transcription. USP21 interacted with GSC to promote GSC deubiquitination while having no effect on GSC protein stability. Cell viability, migration, and function in ATDC5 cells were probably influenced by USP21 through GSC. These findings suggest that USP21 modulates GSC function through deubiquitination.
- Published
- 2019