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  Dicer-dependent and -independent Argonaute2 Protein Interaction Networks in Mammalian Cells

Frohn, A., Eberl, H. C., Stoehr, J., Glasmacher, E., Ruedel, S., Heissmeyer, V., et al. (2012). Dicer-dependent and -independent Argonaute2 Protein Interaction Networks in Mammalian Cells. MOLECULAR & CELLULAR PROTEOMICS, 11(11), 1442-1456. doi:10.1074/mcp.M112.017756.

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 Creators:
Frohn, Anne1, Author              
Eberl, H. Christian1, Author              
Stoehr, Julia2, Author
Glasmacher, Elke2, Author
Ruedel, Sabine2, Author
Heissmeyer, Vigo2, Author
Mann, Matthias1, Author              
Meister, Gunter3, Author              
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
2external, ou_persistent22              
3Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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Free keywords: EMBRYONIC STEM-CELLS; QUANTITATIVE MASS-SPECTROMETRY; MESSENGER-RNA DECAY; TRANSLATIONAL REPRESSION; MICRORNA BIOGENESIS; STRESS GRANULES; MIRNA TARGETS; COMPLEXES; PROTEOMICS; BINDING
 Abstract: Argonaute (Ago) proteins interact with small regulatory RNAs such as microRNAs (miRNAs) and facilitate gene-silencing processes. miRNAs guide Ago proteins to specific mRNAs leading to translational silencing or mRNA decay. In order to understand the mechanistic details of miRNA function, it is important to characterize Ago protein interactors. Although several proteomic studies have been performed, it is not clear how the Ago interactome changes on miRNA or mRNA binding. Here, we report the analysis of Ago protein interactions in miRNA-containing and miRNA-depleted cells. Using stable isotope labeling in cell culture in conjunction with Dicer knock out mouse embryonic fibroblasts, we identify proteins that interact with Ago2 in the presence or the absence of Dicer. In contrast to our current view, we find that Ago-mRNA interactions can also take place in the absence of miRNAs. Our proteomics approach provides a rich resource for further functional studies on the cellular roles of Ago proteins. Molecular & Cellular Proteomics 11: 10.1074/mcp.M112.017756, 1442-1456, 2012.

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Language(s): eng - English
 Dates: 2012-11
 Publication Status: Published in print
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000313277100026
DOI: 10.1074/mcp.M112.017756
 Degree: -

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Title: MOLECULAR & CELLULAR PROTEOMICS
Source Genre: Journal
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Publ. Info: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Pages: - Volume / Issue: 11 (11) Sequence Number: - Start / End Page: 1442 - 1456 Identifier: ISSN: 1535-9476