Proteomics Analysis of the Nucleolus in Adenovirus-infected Cells

Lam, Yun Wah; Evans, Vanessa; Heesom, Kate J; Lamond, Angus I.; Matthews, David A.

doi:10.1074/mcp.m900338-mcp200

Cited by 106 publications

(120 citation statements)

References 64 publications

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“…Nearly 400 proteins were identified within the nucleolar proteome so far in humans, among them eEF1A (43). Moreover, the nucleolar presence of eEF1A was identified in a proteomics analysis of the nucleolus of adenovirus-infected cells (44). It is important to bear in mind that the protein profile of nucleoli is not static because it is modulated by changes in cell physiology.…”

Section: Fig 6 Mutation On Sermentioning

confidence: 99%

eEF1A Phosphorylation in the Nucleus of Insulin-stimulated C2C12 Myoblasts

Piazzi

Bavelloni

Faenza

et al. 2010

Molecular & Cellular Proteomics

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Recent data indicate that some PKC isoforms are translocated to the nucleus, in response to certain stimuli, where they play an important role in nuclear signaling events. To identify novel interacting proteins of conventional PKC (cPKC) at the nuclear level during myogenesis and to find new PKC isozyme-specific phosphosubstrates, we performed a proteomics analysis of immunoprecipitated nuclear samples from mouse myoblast C2C12 cells following insulin administration. Using a phospho(Ser)-PKC substrate antibody, specific interacting proteins were identified by LC-MS/MS spectrometry. A total of 16 proteins with the exact and complete motif recognized by the phospho-cPKC substrate antibody were identified; among these, particular interest was given to eukaryotic elongation factor 1␣ (eEF1A). Nuclear eEF1A was focalized in the nucleoli, and its expression was observed to increase following insulin treatment. Of the cPKC isoforms, only PKC␤I was demonstrated to be expressed in the nucleus of C2C12 myocytes and to coimmunoprecipitate with eEF1A. In-depth analysis using site-directed mutagenesis revealed that PKC␤I could phosphorylate Ser 53 of the eEF1A2 isoform and that the association between eEF1A2 and PKC␤I was dependent on the phosphorylation status of eEF1A2. Molecular & Cellular Proteomics 9:2719 -2728, 2010.

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Section: Fig 6 Mutation On Sermentioning

confidence: 99%

eEF1A Phosphorylation in the Nucleus of Insulin-stimulated C2C12 Myoblasts

Piazzi

Bavelloni

Faenza

et al. 2010

Molecular & Cellular Proteomics

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“…According to the criteria described in the Experimental Procedures, a total of 1498 nonredundant proteins were quantified (Table S1, Supporting Information). In line with common approaches for SILAC analyses, 34,35 we set the threshold for up-or downregulated proteins at 2.0-fold. We found 178 up-regulated and 25 down-regulated proteins in U266 cells 72 h following transfection of LNA-21 (Table S2, Supporting Information).…”

Section: Identification Of Mir-21 Targets Using a Quantitative Proteomentioning

confidence: 99%

Identification of Novel miR-21 Target Proteins in Multiple Myeloma Cells by Quantitative Proteomics

et al. 2012

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Substantial evidence indicates that microRNA-21 (miR-21) is a key oncomiR in carcinogenesis and is significantly elevated in multiple myeloma (MM). In this study, we explored the role of miR-21 in human MM cells and searched for miR-21 targets. By knocking down the expression of endogenous miR-21 in U266 myeloma cells, we observed reduced growth, an arrested cell cycle, and increased apoptosis. To further understand its molecular mechanism in the pathogenesis of MM, we employed a SILAC (stable isotope labeling by amino acids in cell culture)-based quantitative proteomic strategy to systematically identify potential targets of miR-21. In total, we found that the expression of 178 proteins was up-regulated significantly by miR-21 inhibition, implying that they could be potential targets of miR-21. Among these, the protein inhibitor of activated STAT3 (PIAS3) was confirmed as a direct miR-21 target by Western blotting and reporter gene assays. We further demonstrated that miR-21 enhances the STAT3-dependent signal pathway by inhibiting the function of PIAS3 and that down-regulation of PIAS3 contributes to the oncogenic function of miR-21. This elucidation of the role of PIAS3 in the miR-21-STAT3 positive regulatory loop not only may shed light on the molecular basis of the biological effects of miR-21 observed in MM cells but also has direct implications for the development of novel anti-MM therapeutic strategies.

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“…To date, a small but increasing number of studies have used proteomics approaches to reveal the effects of viral infection on the cellular proteome (Maxwell et al, 2007).These include investigations of pseudorabies virus-infected cells (Skiba et al, 2008), coronavirusinfected cells , and alterations to the nucleolar proteome in adenovirus- (Lam et al, 2010) and coronavirus- infected cells. The comparative proteomics approaches coupling 2-DE and MS (2-DE/MS) effectively help the study of the molecular profiles of virus-infected cells.…”

Section: Proteomics Analysis Of Gastric Epithelial Ags Cells Infectedmentioning

confidence: 99%

Proteomics Analysis of Gastric Epithelial AGS Cells Infected with Epstein-Barr Virus

Ding

Li²,

Yang³

et al. 2013

Asian Pacific Journal of Cancer Prevention

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Effects of the Epstein-Barr virus (EBV) on cellular protein expression are essential for viral pathogenesis. To characterize the cellular response to EBV infection, differential proteomes of gastric epithelial AGS cellswere analyzed with two-dimensional gel electrophoresis (2-DE) followed by matrix-assisted laser desorption/ionizationtime of flight (MALDI-TOF) and liquid chromatography electrospray/ionization ion trap (LC-ESI-IT) mass spectrometry identification. Mass spectrometry identified 9 altered cellular proteins, including 5 up-regulated and 4 down-regulated proteins after EBV infection. Notably 2-DE analysis revealed that EBV infection induced increased expression of heat shock cognate 71 kDa protein, actin cytoplasmic 1, pyridoxine-5'-phosphate oxidase, caspase 9, and t-complex protein 1 subunit alpha. In addition, EBV infection considerably suppressed those cellular proteins of zinc finger protein 2, cyclin-dependent kinase 2, macrophage-capping protein, and growth/ differentiation factor 11. Furthermore, the differential expressional levels of partial proteins (cyclin-dependent kinase 2 and caspase 9) were confirmed by Western blot analysis.Thus, this work effectively provided useful protein-related information to facilitate further investigation of the mechanisms underlying EBV infection and pathogenesis.

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Proteomics Analysis of the Nucleolus in Adenovirus-infected Cells

Cited by 106 publications

References 64 publications

eEF1A Phosphorylation in the Nucleus of Insulin-stimulated C2C12 Myoblasts

eEF1A Phosphorylation in the Nucleus of Insulin-stimulated C2C12 Myoblasts

Identification of Novel miR-21 Target Proteins in Multiple Myeloma Cells by Quantitative Proteomics

Proteomics Analysis of Gastric Epithelial AGS Cells Infected with Epstein-Barr Virus

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