QUICK identification and SPR validation of signal transducers and activators of transcription 3 (Stat3) interacting proteins

Zheng, Peng; Zhong, Qian; Xiong, Qian; Yang, Mingkun; Zhang, Jia; Li, Chongyang; Bi, Lijun; Ge, Feng

doi:10.1016/j.jprot.2011.10.020

Cited by 17 publications

(10 citation statements)

References 51 publications

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“…The QUICK method, recently developed by Mann and colleagues (14), is a relatively new method for identifying interactions between proteins at endogenous levels under physiological conditions via a combination of stable isotope labeling with amino acids in cell culture (SILAC), RNA interference (RNAi)-induced knockdown, co-immunoprecipitation, and quantitative MS. This highly sensitive and accurate approach for protein-protein interaction analysis has been applied to identify the interaction partners of ␤-catenin and Cbl (14), 14-3-3 (15), Lrrk2 (16), and Stat3 (17).…”

mentioning

confidence: 99%

Bcl2-associated Athanogene 3 Interactome Analysis Reveals a New Role in Modulating Proteasome Activity

Chen

Yang

Cheng

et al. 2013

Molecular & Cellular Proteomics

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a Bcl2-associated athanogene 3 (BAG3), a member of the BAG family of co-chaperones, plays a critical role in regulating apoptosis, development, cell motility, autophagy, and tumor metastasis and in mediating cell adaptive responses to stressful stimuli. BAG3 carries a BAG domain, a WW domain, and a proline-rich repeat (PXXP), all of which mediate binding to different partners. To elucidate BAG3's interaction network at the molecular level, we employed quantitative immunoprecipitation combined with knockdown and human proteome microarrays to comprehensively profile the BAG3 interactome in humans. We identified a total of 382 BAG3-interacting proteins with diverse functions, including transferase activity, nucleic acid binding, transcription factors, proteases, and chaperones, suggesting that BAG3 is a critical regulator of diverse cellular functions. In addition, we characterized interactions between BAG3 and some of its newly identified partners in greater detail. In particular, bioinformatic analysis revealed that the BAG3 interactome is strongly enriched in proteins functioning within the proteasome-ubiquitination process and that compose the proteasome complex itself, suggesting that a critical biological function of BAG3 is associated with the proteasome. Functional studies demonstrated that BAG3 indeed interacts with the proteasome and modulates its activity, sustaining cell survival and underlying resistance to therapy through the down-modulation of apoptosis. Taken as a whole, this study expands our knowledge of the BAG3 interactome, provides a valuable resource for understanding how BAG3 affects different cellular functions, and demonstrates that biologically relevant data can be harvested using this kind of integrated approach. Molecular

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mentioning

confidence: 99%

Bcl2-associated Athanogene 3 Interactome Analysis Reveals a New Role in Modulating Proteasome Activity

Chen

Yang

Cheng

et al. 2013

Molecular & Cellular Proteomics

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“…It has been fi rst used for the identifi cation of the partners of β-catenin and cbl [ 84 ]. This method has been successfully used to identify the 14-3-3ζ interacting proteins [ 85 ], the leucine-rich repeat kinase 2 interaction partners [ 86 ], to study the molecular functions of the ATP-dependent chromatin remodeling complex SWI/SNF in cell cycle control [ 87 ] and to investigate the role of Stat3 in multiple myeloma pathology [ 88 ].…”

Section: Protein/protein Interactionmentioning

confidence: 99%

Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) for Quantitative Proteomics

Hoedt

Zhang

Neubert

2014

Advances in Experimental Medicine and Biology

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Stable isotope labeling by amino acids in cell culture (SILAC) is a powerful approach for high-throughput quantitative proteomics. SILAC allows highly accurate protein quantitation through metabolic encoding of whole cell proteomes using stable isotope labeled amino acids. Since its introduction in 2002, SILAC has become increasingly popular. In this chapter we review the methodology and application of SILAC, with an emphasis on three research areas: dynamics of posttranslational modifications, protein-protein interactions, and protein turnover.

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“…[4] To assess interaction specificity in studies of endogenous protein complexes, QUICK (quantitative immunoprecipitation combined with knockdown) strategy was developed. [61-64] In this workflow, light-labeled cell cultures are treated with RNAi against the protein of interest, while heavy-labeled cells serve as non-targeted controls. In subsequent MS analysis, light and heavy peptide intensities are compared to assign non-specific (1:1 heavy to light rations) and specific (heavy isotopic peaks with higher intensity than light) interactions.…”

Section: Determining Specificity Of Interactionsmentioning

confidence: 99%

A Mass Spectrometry View of Stable and Transient Protein Interactions

Budayeva

Cristea

2014

Advances in Experimental Medicine and Biology

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QUICK identification and SPR validation of signal transducers and activators of transcription 3 (Stat3) interacting proteins

Cited by 17 publications

References 51 publications

Bcl2-associated Athanogene 3 Interactome Analysis Reveals a New Role in Modulating Proteasome Activity

Bcl2-associated Athanogene 3 Interactome Analysis Reveals a New Role in Modulating Proteasome Activity

Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) for Quantitative Proteomics

A Mass Spectrometry View of Stable and Transient Protein Interactions

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