Predominant Identification of RNA-binding Proteins in Fas-induced Apoptosis by Proteome Analysis

Thiede, Bernd; Dimmler, Christiane; Siejak, Frank; Rudel, Thomas

doi:10.1074/jbc.m101062200

Cited by 122 publications

(106 citation statements)

References 58 publications

(52 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Earlier, we successfully identified novel caspase-3 and caspase-7 substrates using the degradomic approach (Lee et al, 2004;Jang et al, 2007). Thiede et al additionally reported that several proteins, including FBP-1, are modified in Jurkat T cells during apoptosis (Thiede et al, 2001). Data from this study show that FBP-1 is cleaved by caspase-3 and -7, both in vitro and during apoptosis induced by various stimuli.…”

Section: Introductionmentioning

confidence: 53%

Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

et al. 2009

View full text Add to dashboard Cite

Far upstream element-binding protein-1 (FBP-1) binds to an upstream element of the c-myc promoter and regulates the c-myc mRNA level. Earlier, FBP-1 was identified as a candidate substrate of caspase-7. Here, we report that FBP-1 is cleaved by executor caspases, both in vitro and during apoptosis. Cleavage occurs at the caspase consensus site (DQPD 74 ) located within the classical bipartite nuclear localization signal sequence. In cells subjected to apoptotic stimuli, the caspase-mediated cleavage of FBP-1 leads to its decreased presence in the nucleus, concomitant with the marked downregulation of c-Myc and its various target proteins. By contrast, cells transfected with a non-cleavable mutant of FBP-1 (D74A) maintain higher levels of c-Myc and are protected from apoptosis. On the basis of these results, we suggest that the oncogenic potential of c-Myc is 'switched off' after apoptosis induction as a consequence of the caspasemediated cleavage of FBP-1.

show abstract

Section: Introductionmentioning

confidence: 53%

Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

et al. 2009

View full text Add to dashboard Cite

show abstract

“…However, correlation between the results of different studies is usually low. This deviation might be due to differences in cell line, apoptotic inducer, proteomic techniques and experimental design (Thiede et al 2001;Thiede and Rudel 2004). For instance, the heterogeneous nature of non-induced CHO cultures likely influenced our DIGE results, as the populations assayed were composed of cells at different stages.…”

Section: Discussionmentioning

confidence: 99%

Proteomics analysis of chinese hamster ovary cells undergoing apoptosis during prolonged cultivation

et al. 2011

View full text Add to dashboard Cite

The degradation of environmental conditions, such as nutrient depletion and accumulation of toxic waste products over time, often lead to premature apoptotic cell death in mammalian cell cultures and suboptimal protein yield. Although apoptosis has been extensively researched, the changes in the whole cell proteome during prolonged cultivation, where apoptosis is a major mode of cell death, have not been examined. To our knowledge, the work presented here is the first whole cell proteome analysis of non-induced apoptosis in mammalian cells. Flow cytometry analyses of various activated caspases demonstrated the onset of apoptosis in Chinese hamster ovary cells during prolonged cultivation was primarily through the intrinsic pathway. Differential in gel electrophoresis proteomic study comparing protein samples collected during cultivation resulted in the identification of 40 differentially expressed proteins, including four cytoskeletal proteins, ten chaperone and folding proteins, seven metabolic enzymes and seven other proteins of varied functions. The induction of seven ER chaperones and foldases is a solid indication of the onset of the unfolded protein response, which is triggered by cellular and ER stresses, many of which occur during prolonged batch cultures. In addition, the upregulation of six glycolytic enzymes and another metabolic protein emphasizes that a change in the energy metabolism likely occurred as culture conditions degraded and apoptosis advanced. By identifying the intracellular changes during cultivation, this study provides a foundation for optimizing cell line-specific cultivation processes, prolonging longevity and maximizing protein production.

show abstract

“…It has been reported that αNAC may perform certain function in the absence of βNAC (Thiede et al, 2001;Spreter et al, 2005). To study the structure of human αNAC alone, we constructed a number of αNAC variants of different lengths, including the full length and the NAC domain alone (i.e., residues 80-133, named as TαNAC standing for truncated αNAC).…”

Section: Structure Of αNac Nac Domain Homodimermentioning

confidence: 99%

“…In the absence of a hetero-partner, for example when overexpression or downregulation of a single subunit, the remaining dominant subunit may have functions independent of nascent peptide binding (Thiede et al, 2001;Spreter et al, 2005). For instance, isolated αNAC is a multiple functional protein taking part in transcription regulation St-Arnaud, 1998;St-Arnaud and Quelo, 1998;Yotov et al, 1998), cell proliferation, and differentiation (Al-Shanti et al, 2004;Lopez et al, 2005;Al-Shanti and Aldahoodi, 2006).…”

Section: Introductionmentioning

confidence: 99%

Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit

et al. 2010

View full text Add to dashboard Cite

Nascent polypeptide associated complex (NAC) and its two isolated subunits, αNAC and βNAC, play important roles in nascent peptide targeting. We determined a 1.9 Å resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 Å resolution crystal structure of αNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and αNAC homodimerization. We found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a βNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structurefunction relationship of NAC.

show abstract

Predominant Identification of RNA-binding Proteins in Fas-induced Apoptosis by Proteome Analysis

Cited by 122 publications

References 58 publications

Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

Proteomics analysis of chinese hamster ovary cells undergoing apoptosis during prolonged cultivation

Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit

Contact Info

Product

Resources

About