[Ubiquitinated proteomics research of Hep3B].

Abstract

Ubiquitination is one of the most major post-translational modifications playing important role in regulation of intra-cellular proteins' stability, degradation, localization and biological activity. However, these proteins are difficult to be detected due to their low abundance, short half-life. In this study, ubiquitin-binding domains (UBDs) were constructed to purify the ubiquitinated proteins from Hep3B cells. Ubiquitinated proteins and sites were detected by LC-MS/MS. A total of 1 900 potential ubiquitinated proteins were identified. Among them, 158 ubiquitinated sites were identified, belonging to 102 proteins. Bioinformatics analysis revealed that the enriched pathways of ubiquitinated proteins were closely related to tumor occurrence and development. The dysfunction of ubiquitin-proteasome has a high correlation with cell signaling and extracellular matrix changing in tumor cells.

• Authors: Yingzi Qi, Chen Deng, Na Su, Lingqiang Zhang, Ping Xu
• Journal: Sheng wu gong cheng xue bao = Chinese journal of biotechnology (Sheng Wu Gong Cheng Xue Bao) Vol. 32 Issue 10 Pg. 1443-1454 (Oct 25 2016) ISSN: 1000-3061 [Print] China
• PMID: 29027453 (Publication Type: Journal Article)

Chemical References

• Ubiquitinated Proteins
• Proteasome Endopeptidase Complex

Topics

• Half-Life
• Humans
• Proteasome Endopeptidase Complex
• Protein Binding
• Proteomics
• Signal Transduction
• Tandem Mass Spectrometry
• Ubiquitinated Proteins (isolation & purification, metabolism)
• Ubiquitination