Quantitative Phosphoproteomics of Proteasome Inhibition in Multiple Myeloma Cells

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	Quantitative Phosphoproteomics of Proteasome Inhibition in Multiple Myeloma Cells
	Ge, Feng 1,2,3; Xiao, Chuan-Le 1,2; Bi, Li-Jun 4; Tao, Sheng-Ce 5; Xiong, Sheng 1,2; Yin, Xin-Feng 1,2; Li, Li-Ping 1,2; Lu, Chun-Hua 1,2; Jia, Hai-Tao 1,2; He, Qing-Yu 1,2
刊名	PLOS ONE
	2010-09-29
卷号	5 期号:9 页码:-
关键词	PROTEIN-KINASE CK2 MICROTUBULE DYNAMICS SIGNALING NETWORKS AMINO-ACIDS PHOSPHORYLATION AUTOPHAGY PS-341 PROTEOMICS APOPTOSIS BORTEZOMIB
ISSN号	1932-6203
通讯作者	Ge, F, Jinan Univ, Inst Life & Hlth Engn, Guangzhou, Guangdong, Peoples R China
中文摘要	Background: The proteasome inhibitor bortezomib represents an important advance in the treatment of multiple myeloma (MM). Bortezomib inhibits the activity of the 26S proteasome and induces cell death in a variety of tumor cells; however, the mechanism of cytotoxicity is not well understood. Methodology/Principal Findings: We investigated the differential phosphoproteome upon proteasome inhibition by using stable isotope labeling by amino acids in cell culture (SILAC) in combination with phosphoprotein enrichment and LC-MS/MS analysis. In total 233 phosphoproteins were identified and 72 phosphoproteins showed a 1.5-fold or greater change upon bortezomib treatment. The phosphoproteins with expression alterations encompass all major protein classes, including a large number of nucleic acid binding proteins. Site-specific phosphopeptide quantitation revealed that Ser38 phosphorylation on stathmin increased upon bortezomib treatment, suggesting new mechanisms associated to bortezomib-induced apoptosis in MM cells. Further studies demonstrated that stathmin phosphorylation profile was modified in response to bortezomib treatment and the regulation of stathmin by phosphorylation at specific Ser/Thr residues participated in the cellular response induced by bortezomib. Conclusions/Significance: Our systematic profiling of phosphorylation changes in response to bortezomib treatment not only advanced the global mechanistic understanding of the action of bortezomib on myeloma cells but also identified previously uncharacterized signaling proteins in myeloma cells.
英文摘要	Background: The proteasome inhibitor bortezomib represents an important advance in the treatment of multiple myeloma (MM). Bortezomib inhibits the activity of the 26S proteasome and induces cell death in a variety of tumor cells; however, the mechanism of cytotoxicity is not well understood.
学科主题	Biology; Multidisciplinary Sciences
WOS标题词	Science & Technology
类目[WOS]	Multidisciplinary Sciences
研究领域[WOS]	Science & Technology - Other Topics
关键词[WOS]	PROTEIN-KINASE CK2 ; MICROTUBULE DYNAMICS ; SIGNALING NETWORKS ; AMINO-ACIDS ; PHOSPHORYLATION ; AUTOPHAGY ; PS-341 ; PROTEOMICS ; APOPTOSIS ; BORTEZOMIB
收录类别	SCI
资助信息	Chang-Jiang Scholars Program ;
语种	英语
WOS记录号	WOS:000282269400031
公开日期	2010-12-23
内容类型	期刊论文
源URL	[http://ir.ihb.ac.cn/handle/342005/13743]
专题	水生生物研究所_水生生物分子与细胞生物学研究中心_期刊论文
作者单位	1.Jinan Univ, Inst Life & Hlth Engn, Guangzhou, Guangdong, Peoples R China 2.Jinan Univ, Natl Engn Res Ctr Genet Med, Guangzhou, Guangdong, Peoples R China 3.Chinese Acad Sci, Inst Hydrobiol, Wuhan, Peoples R China 4.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China 5.Shanghai Jiao Tong Univ, Shanghai Ctr Syst Biomed, Shanghai 200030, Peoples R China
推荐引用方式 GB/T 7714	Ge, Feng,Xiao, Chuan-Le,Bi, Li-Jun,et al. Quantitative Phosphoproteomics of Proteasome Inhibition in Multiple Myeloma Cells[J]. PLOS ONE,2010,5(9):-.
APA	Ge, Feng.,Xiao, Chuan-Le.,Bi, Li-Jun.,Tao, Sheng-Ce.,Xiong, Sheng.,...&He, Qing-Yu.(2010).Quantitative Phosphoproteomics of Proteasome Inhibition in Multiple Myeloma Cells.PLOS ONE,5(9),-.
MLA	Ge, Feng,et al."Quantitative Phosphoproteomics of Proteasome Inhibition in Multiple Myeloma Cells".PLOS ONE 5.9(2010):-.