The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin
Open accessAbstract
Synthesis of many proteins is tightly controlled at the level of translation, and plays an essential role in fundamental processes such as cell growth and proliferation, signaling, differentiation, or death. Methods that allow imaging and identification of nascent proteins are critical for dissecting regulation of translation, both spatially and temporally, particularly in whole organisms. We introduce a simple and robust chemical method to image and affinity-purify nascent proteins in cells and in animals, based on an alkyne analog of puromycin, O-propargyl-puromycin (OP-puro). OP-puro forms covalent conjugates with nascent polypeptide chains, which are rapidly turned over by the proteasome and can be visualized or captured by copper(I)-catalyzed azide-alkyne cycloaddition. Unlike methionine analogs, OP-puro does not require methionine-free conditions and, uniquely, can be used to label and assay nascent proteins in whole organisms. This strategy should have broad applicability for imaging protein synthesis and for identifying proteins synthesized under various physiological and pathological conditions in vivo.
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Cites
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Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
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The impact of microRNAs on protein output
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“In particular, OP-puro should allow the identification of proteins regulated at the level of translation, such as targets of specific micro-RNAs (2, 3), targets of other RNA-binding proteins that control translation of specific mRNAs, and targets of signaling pathways that regulate translation.”
BackgroundRegulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
Sonenberg, N., & Hinnebusch, A. G. (2009) · Cell · doi:10.1016/j.cell.2009.01.042 · Cited by 3,304
A chemical method for fast and sensitive detection of DNA synthesis in vivo
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Self-citationSUnSET, a nonradioactive method to monitor protein synthesis
Schmidt, E. K., Clavarino, G., Ceppi, M., & Pierre, P. (2009) · Nature Methods · doi:10.1038/nmeth.1314 · Cited by 1,706
Bioconjugation by Copper(I)-Catalyzed Azide-Alkyne [3 + 2] Cycloaddition
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Cited by
Llorens-Bobadilla, E., Zhao, S., Baser, A., Saiz-Castro, G., Zwadlo, K., & Martin-Villalba, A. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2015.07.002 · Cited by 778
Haematopoietic stem cells require a highly regulated protein synthesis rate
Signer, R. A. J., Magee, J. A., Salic, A., & Morrison, S. J. (2014) · Nature · doi:10.1038/nature13035 · Cited by 674
Self-citationm6A facilitates hippocampus-dependent learning and memory through YTHDF1
Shi, H., Zhang, X., Weng, Y.-L., Lu, Z., Liu, Y., Lu, Z., Li, J., Hao, P., Zhang, Y., Zhang, F., et al. (2018) · Nature · doi:10.1038/s41586-018-0666-1 · Cited by 546
Haas, S., Hansson, J., Klimmeck, D., Loeffler, D., Velten, L., Uckelmann, H., Wurzer, S., Prendergast, Á. M., Schnell, A., Hexel, K., et al. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2015.07.007 · Cited by 471
Vitamin A-Retinoic Acid Signaling Regulates Hematopoietic Stem Cell Dormancy
Cabezas-Wallscheid, N., Buettner, F., Sommerkamp, P., Klimmeck, D., Ladel, L., Thalheimer, F. B., Pastor-Flores, D., Roma, L. P., Renders, S., Zeisberger, P., et al. (2017) · Cell · doi:10.1016/j.cell.2017.04.018 · Cited by 454
Metadata
- Authors
- Liu, J., Xu, Y., Stoleru, D., & Salic, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-12-12
- Volume
- 109
- Issue
- 2
- Pages
- 413-418
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2132051882
- Cited by
- 447
- References
- 29
- FWCI
- 3.89
- Type
- journal article
- Language
- en
- Open access
- bronze
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