The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Both G 3 BP 1 and G 3 BP 2 contribute to stress granule formation
Abstract
Upon exposure to various environmental stresses such as arsenite, hypoxia, and heat shock, cells inhibit their translation and apoptosis and then repair stress‐induced alterations, such as DNA damage and the accumulation of misfolded proteins. These types of stresses induce the formation of cytoplasmic RNA granules called stress granules (SG s). SGs are storage sites for the many mRNA s released from disassembled polysomes under these stress conditions and are essential for the selective translation of stress‐inducible genes. Ras‐GTP ase‐activating protein SH 3 domain‐binding protein 1 (G 3 BP 1) is a component of SG s that initiates the assembly of SG s by forming a multimer. In this study, we examined the role of G 3 BP 2, a close relative of G3BP 1, in SG formation. Although single knockdown of either G3BP1 or G3BP2 in 293 T cells partially reduced the number of SG‐positive cells induced by arsenite, the knockdowns of both genes significantly reduced the number. G 3 BP 2 formed a homo‐multimer and a hetero‐multimer with G3BP1. Moreover, like G 3 BP 1, the overexpression of G 3 BP 2 induced SG s even without stress stimuli. Collectively, these results suggest that both G 3 BP 1 and G 3 BP 2 play a role in the formation of SG s in various human cells and thereby recovery from these cellular stresses.
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1 retracted
RETRACTED: The RasGAP-associated endoribonuclease G3BP assembles stress granules
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RetractedDefining the Human Deubiquitinating Enzyme Interaction Landscape
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Stress granules: the Tao of RNA triage
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RNA granules: post-transcriptional and epigenetic modulators of gene expression
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Dynamic Shuttling of Tia-1 Accompanies the Recruitment of mRNA to Mammalian Stress Granules
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Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
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G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits
Kedersha, N., Panas, M. D., Achorn, C. A., Lyons, S., Tisdale, S., Hickman, T., Thomas, M., Lieberman, J., McInerney, G. M., Ivanov, P., et al. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201508028 · Cited by 659
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Metadata
- Authors
- Matsuki, H., Takahashi, M., Higuchi, M., Makokha, G. N., Oie, M., & Fujii, M.
- Venue
- Genes to Cells
- Publisher
- Wiley
- Published
- 2012-12-26
- Volume
- 18
- Issue
- 2
- Pages
- 135-146
- ISSN
- 1356-9597 (ISSN-L)
- 1365-2443
- OpenAlex
- W2078779212
- Cited by
- 300
- References
- 22
- FWCI
- 4.41
- Type
- journal article
- Language
- en
- Open access
- closed
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