ArticleProceedings of the National Academy of Sciences of the United States of America2004
Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 69 citations in OpenAlex.
- Single-Step Purification of Endogenous Human Chaperonin CCT.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Mapping the chaperonin TRiC/CCT interactome in mouse photoreceptors reveals functional significance for energy metabolism.PloS one · 2026Article
- The oncolytic avian reovirus p17 protein triggers chaperone-mediated autophagy by modulating Hsp90 and the T-complex protein-1 ring complex chaperones and co-chaperones to activate the IKK/NF-κB signaling.Journal of virology · 2025Article
- A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle.Nature communications · 2024Article
- The evolutionarily conserved PhLP3 is essential for sperm development in Drosophila melanogaster.PloS one · 2024Article
- Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller.Molecular cell · 2023Article
- Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.Science advances · 2023Article
- PDCL2 is essential for spermiogenesis and male fertility in mice.Cell death discovery · 2022Article
- The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022Review
- Characterization of a protozoan Phosducin-like protein-3 (PhLP-3) reveals conserved redox activity.PloS one · 2018Article
- The Mechanism and Function of Group II Chaperonins.Journal of molecular biology · 2015Review
- Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Splice isoforms of phosducin-like protein control the expression of heterotrimeric G proteins.The Journal of biological chemistry · 2013Article
- Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.The Journal of biological chemistry · 2013Article
- The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning.Structure (London, England : 1993) · 2013Article
- The molecular architecture of the eukaryotic chaperonin TRiC/CCT.Structure (London, England : 1993) · 2012Article
- The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.The EMBO journal · 2011Article
- Modulation of phosducin-like protein 3 (PhLP3) levels promotes cytoskeletal remodelling in a MAPK and RhoA-dependent manner.PloS one · 2011Article
- Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Journal of amino acids · 2011Article
- Disruption of the chaperonin containing TCP-1 function affects protein networks essential for rod outer segment morphogenesis and survival.Molecular & cellular proteomics : MCP · 2011Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The three-dimensional structure of the complex formed between the cytosolic chaperonin CCT (chaperonin containing TCP-1) and phosducin (Pdc)-like protein (PhLP), a regulator of CCT activity, has been solved by cryoelectron microscopy. Binding of PhLP to CCT occurs through only one of the chaperonin rings, and the protein does not occupy the central folding cavity but rather sits above it through interactions with two regions on opposite sides of the ring. This causes the apical domains of the CCT subunits to close in, thus excluding access to the folding cavity. The atomic model of PhLP generated from several atomic structures of the homologous Pdc fits very well with the mass of the complex attributable to PhLP and predicts the involvement of several sequences of PhLP in CCT binding. Binding experiments performed with PhLP/Pdc chimeric proteins, taking advantage of the fact that Pdc does not interact with CCT, confirm that both the N- and C-terminal domains of PhLP are involved in CCT binding and that several regions suggested by the docking experiment are indeed critical in the interaction with the cytosolic chaperonin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.