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Both G 3 BP 1 and G 3 BP 2 contribute to stress granule formation
Author(s) -
Matsuki Hideaki,
Takahashi Masahiko,
Higuchi Masaya,
Makokha Grace N,
Oie Masayasu,
Fujii Masahiro
Publication year - 2013
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12023
Subject(s) - stress granule , microbiology and biotechnology , biology , p bodies , gene knockdown , heat shock protein , messenger rna , translation (biology) , gene , biochemistry
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.