What are interactors of the TRiC/CCT chaperonin?
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The TRiC/CCT chaperonin interacts with various proteins in different cellular processes. It has been shown to interact with G protein β subunits (Gβ) for G protein complex assembly , assist in the folding of cytoskeletal proteins like tubulin and actin , and play a crucial role in the life cycle of viruses such as dengue, Zika, influenza, and mammarenaviruses like LCMV, JUNV, and LASV . Additionally, the TRiC/CCT complex interacts with co-chaperones like phosducin-like protein 1 (PhLP1) to facilitate the folding of Gβ subunits . These interactions highlight the diverse functions of the TRiC/CCT chaperonin in protein folding, viral multiplication, and cellular processes.
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|---|---|
| Interactors of TRiC/CCT chaperonin include co-chaperone plp2, tubulin, and actin, facilitating their folding process and coordination within TRiC chambers during the adenosine triphosphatase cycle. | |
26 Mar 2022 | The TRiC/CCT chaperonin interacts with β-tubulin intermediates, establishing specific contacts with the N-domain, C-terminal E-hook tail, Core, Middle domains, and GTP-binding regions during the folding pathway. |
| Interactors of TRiC/CCT chaperonin include cochaperone plp2, assisting in folding cytoskeletal proteins tubulin and actin, as revealed by cryo-EM analysis in different states of the ATPase cycle. | |
2 Citations | Interactors of the TRiC/CCT chaperonin include the nucleoprotein (NP) of mammarenavirus LCMV, essential for virus multiplication, as highlighted in the research paper. |
| Interactors of the TRiC/CCT chaperonin include G protein β5 subunit and its co-chaperone PhLP1, crucial for folding Gβ into β-propeller structures for G protein complex assembly. |
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