Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc   regulates box C/D snoRNP biogenesis

doi:10.1073/pnas.1702688114

CORC > 北京大学 > 化学与分子工程学院

	Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesis
	Qin, Wei ; Lv, Pinou ; Fan, Xinqi ; Quan, Baiyi ; Zhu, Yuntao ; Qin, Ke ; Chen, Ying ; Wang, Chu ; Chen, Xing
刊名	PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
	2017
关键词	O-GlcNAcylation metabolic labeling proteomics protein stability snoRNP MODIFIED PROTEINS MASS-SPECTROMETRY RIBOSOMAL-RNA TRANSLATIONAL CONTROL BIOSYNTHETIC-PATHWAY CIRCADIAN CLOCK CHRONIC DISEASE H/ACA SNORNPS BREAST-CANCER CROSS-TALK
DOI	10.1073/pnas.1702688114
英文摘要	O-linked GlcNAcylation (O-GlcNAcylation), a ubiquitous posttranslational modification on intracellular proteins, is dynamically regulated in cells. To analyze the turnover dynamics of O-GlcNAcylated proteins, we developed a quantitative time-resolved O-linked GlcNAc proteomics (qTOP) strategy based on metabolic pulse-chase labeling with an O-GlcNAc chemical reporter and stable isotope labeling with amino acids in cell culture (SILAC). Applying qTOP, we quantified the turnover rates of 533 O-GlcNAcylated proteins in NIH 3T3 cells and discovered that about 14% exhibited minimal removal of O-GlcNAc or degradation of protein backbones. The stability of those hyperstable O-GlcNAcylated proteins was more sensitive to O-GlcNAcylation inhibition compared with the more dynamic populations. Among the hyperstable population were three core proteins of box C/D small nucleolar ribonucleoprotein complexes (snoRNPs): fibrillarin (FBL), nucleolar protein 5A (NOP56), and nucleolar protein 5 (NOP58). We showed that O-GlcNAcylation stabilized these proteins and was essential for snoRNP assembly. Blocking O-GlcNAcylation on FBL altered the 2'-O-methylation of rRNAs and impaired cancer cell proliferation and tumor formation in vivo.; National Natural Science Foundation of China [21472008, 81490740, 21425204, 21521003, 21672013]; National Key Research and Development Projects Grant [2016YFA0501500]; "1000 Talents Plan" Young Investigator Award; SCI(E); ARTICLE; 33; E6749-E6758; 114
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/471461]
专题	化学与分子工程学院生命科学学院
推荐引用方式 GB/T 7714	Qin, Wei,Lv, Pinou,Fan, Xinqi,et al. Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesis[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2017.
APA	Qin, Wei.,Lv, Pinou.,Fan, Xinqi.,Quan, Baiyi.,Zhu, Yuntao.,...&Chen, Xing.(2017).Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesis.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA.
MLA	Qin, Wei,et al."Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesis".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2017).