The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
Open accessAbstract
Processing bodies (P-bodies) are cytoplasmic RNA granules that contain translationally repressed messenger ribonucleoproteins (mRNPs) and messenger RNA (mRNA) decay factors. The physical interactions that form the individual mRNPs within P-bodies and how those mRNPs assemble into larger P-bodies are unresolved. We identify direct protein interactions that could contribute to the formation of an mRNP complex that consists of core P-body components. Additionally, we demonstrate that the formation of P-bodies that are visible by light microscopy occurs either through Edc3p, which acts as a scaffold and cross-bridging protein, or via the “prionlike” domain in Lsm4p. Analysis of cells defective in P-body formation indicates that the concentration of translationally repressed mRNPs and decay factors into microscopically visible P-bodies is not necessary for basal control of translation repression and mRNA decay. These results suggest a stepwise model for P-body assembly with the initial formation of a core mRNA–protein complex that then aggregates through multiple specific mechanisms.
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Cites
Anderson, P., & Kedersha, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512082 · Cited by 984
P-body formation is a consequence, not the cause, of RNA-mediated gene silencing
Eulalio, A., Behm-Ansmant, I., Schweizer, D., & Izaurralde, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00128-07 · Cited by 710
Cited by
(2008) · doi:10.1038/nrg2290 · Cited by 5,199
Regulation of mRNA Translation and Stability by microRNAs
Fabian, M. R., Sonenberg, N., & Filipowicz, W. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060308-103103 · Cited by 3,214
Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012
Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803
Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C. C.-H., Eckmann, C. R., Myong, S., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504822112 · Cited by 1,278
Metadata
- Authors
- Decker, C. J., Teixeira, D., & Parker, R.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2007-11-05
- Volume
- 179
- Issue
- 3
- Pages
- 437-449
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2146865209
- Cited by
- 467
- References
- 2
- FWCI
- 9.46
- Type
- journal article
- Language
- en
- Open access
- green
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- Decker, C. J., Teixeira, D., & Parker, R. (2007). Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200704147
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