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The force-dependent filamin A-G3BP1 interaction regulates phase-separated stress granule formation

J Cell Sci. 2023-03; 
Ziyi Feng, Zhenfeng Mao, Ziwei Yang, Xiaowei Liu, Fumihiko Nakamura
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Proteins, Expression, Isolation and Analysis … The fusion protein was purified from the supernatant using high affinity Ni-NTA beads (GenScript). After cleavage of the His tag with tobacco etch virus (TEV) protease, the protein was … Get A Quote

摘要

Filamin A (FLNA) is an actin crosslinking protein that mediates mechanotransduction. External and internal mechanical forces, through the actin cytoskeleton, can induce conformational changes of the FLNA molecule to expose cryptic binding sites for its binding partners. Here, we identified Ras GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) as a new FLNA mechanobinding partner. Unlike other FLNA binding partners to the mechanosensing domain repeat 21 (R21), G3BP1 requires an additional neighboring repeat R22 to interact. We demonstrated that their interaction occurs in the cytosol of living cells in an actin polymerization-dependent manner. We also mapped the FLNA-binding site on G3BP1 and found ... More

關(guān)鍵詞

Cytoskeleton, FLNA, Filamin A, G3BP1, Mechanotransduction, Phase separation, Ras GTPase-activating protein-binding protein 1, Stress granule
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