Stress granule

Kedersha, N., Stoecklin, G., Ayodele, M., Yacono, P., Lykke-Andersen, J., Fritzler, M. J., Scheuner, D., Kaufman, R. J., Golan, D. E., and Anderson, P. (2005). Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J. Cell Biol. 169, 871-884. 

Baez, M. V., and Boccaccio, G. L. (2005). Mammalian Smaug is a translational repressor that forms cytoplasmic foci similar to stress granules. J. Biol. Chem. 280, 43131—43140. 

Dang, Y., Kedersha, N., Low, W. K., Romo, D., Gorospe, M., Kaufman, R., Anderson, P., and Liu, J. O. (2006). Eukaryotic initiation factor 2alpha-independent pathway of stress granule induction by the natural product pateamine A. J. Biol. Chem. 281, 32870-32878. 

Hofmann, I., Casella, M., Schnolzer, M., Schlechter, T., Spring, H., and Franke, W. W. (2006). Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules. Mol. Biol. Cell 17, 1388—1398. 

Hua, Y., and Zhou, J. (2004). Survival motor neuron protein facilitates assembly of stress granules. FEBS Lett. 572, 69-74. 

Kedersha, N., Chen, S., Gilks, N., Li, W., Miller, I. J., Stahl, J., and Anderson, P. (2002). Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol. Biol. Cell 13, 195—210. 

Kim, W. J., Back, S. H., Kim, V., Ryu, I., andjang, S. K. (2005). Sequestration ofTRAF2 into stress granules interrupts tumor necrosis factor signaling under stress conditions. Mol. Cell Biol. 25, 2450-2462. 

Mazroui, R., Sukarieh, R., Bordeleau, M. E., Kaufman, R. J., Northcote, P., Tanaka, J., Gallouzi, I., and Pelletier, J. (2006). Inhibition of ribosome recruitment induces stress granule formation independendy of eukaryotic initiation factor 2alpha phosphorylation. Mol. Biol. Cell 17, 4212-4219. 

Stoecklin, G., Stubbs, T., Kedersha, N., Blackwell, T. K., and Anderson, P. (2004). MK2-induced tristetraprolin 14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 23, 1313-1324. 

Tourriere, H., Chebli, K., Zekri, L., Courselaud, B., Blanchard, J. M., Bertrand, E., and Tazi, J. (2003). The RasGAP-associated endoribonuclease G3BP assembles stress granules. J. Cell Biol. 160, 823—831. 

Wilczynska, A., Aigueperse, C., Kress, M., Dautry, F., and Weil, D. (2005). The translational regulator CPEB1 provides a link between dcpl bodies and stress granules. J. Cell Sci. 118, 981-992. 

Yang, F., Peng, Y., Murray, E. L., Otsuka, Y., Kedersha, N., and Schoenberg, D. R. (2006). Polysome-bound endonuclease PMR1 is targeted to stress granules via stress-specific binding to TIA-1. Mol. Cell Biol. 26, 8803—8813. 

Leung, A. K., Calabrese, J. M., and Sharp, P. A. (2006). Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules. Proc. Natl. Acad. Sci. L7 4 103, 18125-18130. 

Moeller BJ, Cao Y, Li CY, Dewhirst MW. Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors role of reoxygenation, free radicals, and stress granules. Cancer Cell 2004 5 429-441. 

Miroshnichenko, S. et al. (2005) Immuno-modulation of function of small heat shock proteins prevents their assembly into heat stress granules and results in cell death at sublethal temperatures. Plant J. 41, 269-281... 

---