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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P39078
• Protein Description: RecName: Full=T-complex protein 1 subunit delta; Short=TCP-1-delta; AltName: Full=CCT-delta;
• Gene Information: Name=CCT4; Synonyms=ANC2, TCP4; OrderedLocusNames=YDL143W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_delta. (IPR012717); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS. (IPR002194); Cpn60/GroEL/TCP-1. (IPR002423); GroEL-like_apical_dom_sf. (IPR027409)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CCT4" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'CCT4' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene CCT4 (gene ID: CCT4, UniProt: P39078) in yeast.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: P39078
• Protein Description: RecName: Full=T-complex protein 1 subunit delta; Short=TCP-1-delta; AltName: Full=CCT-delta;
• Gene Information: Name=CCT4; Synonyms=ANC2, TCP4; OrderedLocusNames=YDL143W;
• Organism (full): Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Protein Family: Belongs to the TCP-1 chaperonin family. .
• Key Domains: Chap_CCT_delta. (IPR012717); Chaperone_TCP-1. (IPR017998); Chaperonin_TCP-1_CS. (IPR002194); Cpn60/GroEL/TCP-1. (IPR002423); GroEL-like_apical_dom_sf. (IPR027409)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CCT4" matches the protein description above
2. Verify the organism is correct: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'CCT4' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene CCT4 (gene ID: CCT4, UniProt: P39078) in yeast.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Comprehensive research report: Saccharomyces cerevisiae CCT4 (UniProt P39078; YDL143W)

0) Target verification (mandatory)

The research target is Saccharomyces cerevisiae (S288c) CCT4 (ordered locus YDL143W; UniProt P39078), encoding T-complex protein 1 subunit delta (Cct4p), a subunit of the eukaryotic cytosolic group II chaperonin TRiC/CCT (also called TCP-1 ring complex). This identity is consistent with yeast structural subunit-mapping that directly labels CCT4 within the TRiC ring and with authoritative reviews that list CCT4 among the canonical CCT1–CCT8 subunits. (zang2018developmentofa pages 3-5, shen2025proteinfoldingby pages 1-3)

1) Key concepts and definitions (current understanding)

1.1 TRiC/CCT is a group II chaperonin (folding machine), not an enzyme

Cct4p is not an enzyme with a discrete chemical reaction; it is a structural and catalytic (ATPase-driven) component of a molecular chaperonin that promotes ATP-dependent folding of specific cytosolic proteins inside a central chamber. TRiC/CCT is a ~1 MDa complex comprising 16 subunits arranged as two stacked rings of eight distinct subunits (CCT1–CCT8). (que2024theroleof pages 2-4, willison2018thesubstratespecificity pages 1-2)

1.2 ATP-driven open/closed cycle and subunit specialization

TRiC/CCT operates via an ATP-driven open↔closed cycle: substrates bind in the open state, ATP binding and hydrolysis drive large conformational rearrangements that close the chamber to constrain the folding landscape, and reopening releases folded substrates. (que2024theroleof pages 2-4, shen2025proteinfoldingby pages 1-3)

A key aspect of current understanding is functional asymmetry among the eight subunits. CCT4 is repeatedly classified among higher ATP-affinity subunits (along with CCT1, CCT2, CCT5), consistent with subunit-specialized ATP handling within the ring and staggered allostery. (shen2025proteinfoldingby pages 1-3, dube2021chaperoninpointmutation pages 1-4)

2) CCT4-specific structural position in yeast TRiC/CCT (direct evidence)

2.1 Yeast cryo-EM subunit assignment using internal eGFP labeling (YISEL)

A yeast-specific cryo-EM strategy (YISEL: internal-subunit eGFP labeling) inserted eGFP into Cct4p and reconstructed TRiC in the open NPP state, enabling unambiguous localization of CCT4 within the 8-subunit ring. CCT4 is positioned adjacent to CCT2 and assigned as subunit a2 in the ring model. (zang2018developmentofa pages 3-5)

The corresponding cryo-EM images directly show the CCT4-eGFP density and the full TRiC subunit arrangement (supporting the CCT4=a2 claim). (zang2018developmentofa media f48bc63a, zang2018developmentofa media 2d323812)

3) Primary biological function of yeast CCT4 (functional annotation)

3.1 Core function: proteostasis via folding of selected cytosolic clients

The dominant, experimentally supported functional role of CCT/TRiC in yeast is folding of cytoskeletal proteins and a selective set of additional complex-topology proteins.

Canonical/obligate substrates (client proteins):
- Actin: CCT catalyzes folding to assembly-competent G-actin in yeast; actin is described as an obligate CCT substrate. (willison2018thesubstratespecificity pages 2-3, willison2018thesubstratespecificity pages 6-6)
- Tubulin: CCT is involved in tubulin biogenesis/folding; structural work supports subunit-resolved interactions during tubulin folding intermediates. (nadlerholly2012interactionsofsubunit pages 5-6, shen2025proteinfoldingby pages 1-3)
- WD40/β-propeller proteins: Yeast APC/C activators Cdc20p and Cdh1p are described as CCT-dependent, with in vivo folding/activation requiring CCT and mutational mapping of CCT-binding determinants in propeller blades (client-level specificity). (willison2018thesubstratespecificity pages 6-6, willison2018thesubstratespecificity pages 1-2)

CCT4-specific client contact evidence (highest specificity available in the retrieved set):
A structural review summarizing cryo-EM and biochemical work reports that tubulin early folding intermediates form electrostatic contacts with CCT4 (among other subunits), supporting a direct role for CCT4 in tubulin folding trajectories. (shen2025proteinfoldingby pages 1-3)

3.2 Essentiality and growth phenotypes linked to CCT4 function

Multiple yeast-focused sources describe that the eight CCT genes are essential, and that perturbations of ATP-binding/hydrolysis motifs yield severe growth defects or loss of viability. (willison2018thesubstratespecificity pages 2-3)

CCT4-specific genetic/phenotypic evidence includes:
- A CCT4 G345D mutation abolishes ATP-induced allostery and renders yeast temperature-sensitive for growth, demonstrating that proper CCT4 allosteric function is required for normal growth. (nadlerholly2012interactionsofsubunit pages 5-6)
- In yeast cct4 temperature-sensitive (cct4-ts) strains (used in an aggrephagy study), cells grow at 30°C but are lethal at 37°C; these mutants disrupt TRiC integrity as assayed by reduced α-tubulin at restrictive temperature—linking Cct4 function to cytoskeletal proteostasis and complex stability under stress. (chen2024twodistinctregulatory pages 3-5)

4) Subcellular localization and site of action

4.1 Cytosolic localization (canonical)

TRiC/CCT is consistently described as a cytoplasmic/cytosolic chaperonin in yeast, consistent with its major folding clients (actin/tubulin) and with reviews describing CCT subunits as having median concentrations “throughout the cytoplasm.” (nadlerholly2012interactionsofsubunit pages 5-6, willison2018thesubstratespecificity pages 7-8)

4.2 Nuclear pool and nuclear function (recent yeast evidence)

A 2024 yeast preprint reports a nuclear role for TRiC/CCT in regulating RNA polymerase II (RNAPII) activity and maintaining RNA homeostasis. The study uses a cct1-2 mutant, nuclear depletion strategies for GFP-tagged CCT subunits, genome-wide nascent transcription (4tU-Seq), RNA-Seq, chromatin accessibility assays, histone tail PTM mass spectrometry, and in vitro transcription using nuclear extracts. Together, these data support a model in which a nuclear fraction of TRiC/CCT affects transcription termination/readthrough and RNA production/stability. Although not CCT4-specific, it extends the functional landscape of yeast TRiC/CCT beyond cytosolic folding. (gvozdenov2024triccctchaperoningoverns pages 21-25, gvozdenov2024triccctchaperoningoverns pages 30-33)

5) Pathways and biological processes linked to CCT4 (evidence-based)

5.1 Cytoskeleton organization and cell cycle control

CCT/TRiC’s yeast clients and phenotypes strongly connect it to actin and microtubule biology and to cell-cycle regulation, including folding/assembly of APC/C activators (Cdc20p/Cdh1p) and mention of essential proteins including regulators of cell division. (nadlerholly2012interactionsofsubunit pages 1-2, willison2018thesubstratespecificity pages 6-6)

5.2 Stress tolerance and proteostasis under heat stress

The temperature-sensitive lethality of cct4-ts at 37°C and α-tubulin reduction at restrictive temperature provide direct evidence that CCT4 supports proteostasis under heat stress, consistent with TRiC’s broader role in stress resilience. (chen2024twodistinctregulatory pages 3-5)

5.3 Selective autophagy/aggrephagy context (CCT4 used as a TRiC integrity perturbation)

A 2024 EMBO Reports study of “solid aggrephagy” identifies Cct2 (not Cct4) as an Atg8-binding receptor-like factor, and shows that Atg8 binds exclusively to free Cct2 rather than Cct1/Cct4. In that context, cct4-ts is used as a perturbation that disrupts TRiC complex integrity, but Cct4 itself is not the Atg8-binding factor in the reported assays. (chen2024twodistinctregulatory pages 5-7, chen2024twodistinctregulatory pages 3-5)

6) Quantitative statistics and data points (yeast-focused, recent where possible)

6.1 Cct4 protein abundance (copies per cell)

Absolute proteomics (QconCAT/SRM) quantified Cct4 ≈ 20,000 ± 1,000 copies per cell in budding yeast under the tested condition, placing it among the more abundant CCT subunits in that dataset. (brownridge2013quantitativeanalysisof pages 5-6)

6.2 CCT4 transcript abundance and coordinated expression

A yeast-centered systems analysis summarized CCT4 mRNA ≈ 2.16 copies per cell (low absolute copy number but coordinated across CCT subunits), consistent with tight stoichiometric control for assembly of the hetero-oligomeric complex. (willison2018thesubstratespecificity pages 7-8)

6.3 Estimated CCT complexes per cell

The same review context estimates yeast has on the order of ~3,000–6,000 CCT complexes per cell, contextualizing folding capacity relative to obligate high-abundance clients (actin/tubulin). (willison2018thesubstratespecificity pages 6-6)

6.4 Quantitative kinetic parameters from yeast TRiC disease-mutation modeling (contextual)

Although focused on CCT2, yeast kinetic studies provide quantitative parameters illustrating TRiC enzymology (ATPase cycle): e.g., kcat values on the order of ~0.04–0.05 s−1 and ATP-dependent behavior consistent with altered ADP off-rate in disease-linked mutants. These results inform how subunit-specific perturbations (including those affecting allostery, like CCT4 G345D) can plausibly alter the global duty cycle. (roy2023reducedadpoffrate pages 1-2)

7) Recent developments and latest research (prioritized 2023–2024)

7.1 2024 Nature Communications: CCT4 as a conserved cochaperone interaction surface (PhLP2A/PFD)

A major 2024 advance is a high-resolution structural and biochemical dissection of TRiC cooperation with PhLP2A and prefoldin (PFD). The study reports that:
- PFD preferentially binds an apical site on CCT4, whereas PhLP2A binds multivalently, including apical sites on CCT3/4 and additional contacts that enable it to remain bound during closure. (junsun2024astructuralvista pages 3-4)
- Crosslinking-MS and cryo-EM support direct PhLP2A contacts with CCT4 (apical and cavity-facing regions), and PhLP2A H3 binding to CCT3/4 can displace PFD from TRiC. (junsun2024astructuralvista pages 1-2)
- A conserved charged patch on CCT4 is described as functionally important for proteostasis, as mutation impairs cellular proteostasis (reported in the 2024 paper’s analysis). (junsun2024astructuralvista pages 3-4)

This is directly relevant to yeast Cct4 annotation because it strengthens a mechanistic view in which CCT4 is not only a folding chamber subunit but also a key docking surface for upstream cochaperones that govern substrate delivery and cycle timing. (junsun2024astructuralvista pages 3-4)

7.2 2024 EMBO Reports: cct4-ts as a TRiC integrity perturbation linked to tubulin levels

In yeast, cct4-ts strains are explicitly used to disrupt TRiC integrity; at restrictive temperature they show reduced α-tubulin and lethality, tying TRiC stability (and thus Cct4 function) to cytoskeletal client maintenance in vivo. (chen2024twodistinctregulatory pages 3-5)

7.3 2024 bioRxiv (yeast): TRiC/CCT in RNAPII regulation and RNA homeostasis

A 2024 yeast preprint proposes a direct nuclear role of TRiC/CCT in RNAPII activity, termination/readthrough, chromatin features (including altered H2A.Z occupancy), and RNA half-life behavior using integrated genome-wide assays and in vitro transcription. (gvozdenov2024triccctchaperoningoverns pages 21-25)

7.4 2024 Heliyon review: TRiC/CCT and translation elongation (synthesis–folding coupling)

A 2024 literature review focuses on TRiC/CCT in translation elongation and reiterates quantitative framing that TRiC contributes to folding of ~10% of cytosolic proteins and functions via ATP-driven chamber closure. While not yeast CCT4-specific, it represents a recent consolidation of mechanistic understanding and provides up-to-date synthesis for the translation–folding interface. (que2024theroleof pages 2-4)

8) Current applications and real-world implementations

8.1 Yeast as an experimental platform for chaperonin biology and subunit assignment

CCT4 has been used as a target for internal tagging and cryo-EM subunit identification in yeast, demonstrating a practical methodology for mapping subunit order in hetero-oligomeric assemblies at intermediate resolution. This is a real-world implementation enabling reproducible structural assignment in complex machines. (zang2018developmentofa pages 2-3, zang2018developmentofa pages 3-5)

8.2 Yeast TRiC as a model for interpreting human disease mechanisms

Yeast TRiC subunits (particularly CCT2 in the retrieved evidence) are used to model human disease mutations with quantitative kinetics, illustrating how yeast provides a tractable system to dissect chaperonin duty cycles and allostery. This general approach is conceptually relevant to CCT4 because subunit-specific allosteric defects (like CCT4 G345D) can be studied analogously. (roy2023reducedadpoffrate pages 1-2, nadlerholly2012interactionsofsubunit pages 5-6)

9) Expert synthesis and interpretation (evidence constrained)

1. Primary functional annotation for yeast CCT4: Cct4p is best annotated as an essential cytosolic chaperonin subunit whose principal role is to enable ATP-driven folding of a selective set of cytosolic proteins (notably cytoskeletal clients) and to integrate into a precisely ordered TRiC ring with subunit-specific ATP properties. (willison2018thesubstratespecificity pages 2-3, shen2025proteinfoldingby pages 1-3)

2. CCT4 appears to be a key “interface subunit” in the broader chaperone network: structural and XL-MS evidence indicates CCT4 provides conserved surfaces for cochaperone binding (PFD and PhLP2A), which plausibly shapes client delivery and cycle transitions. (junsun2024astructuralvista pages 3-4, junsun2024astructuralvista pages 1-2)

3. Phenotype-based evidence suggests allosteric integrity is essential: the CCT4 G345D allostery-disrupting mutation causing temperature-sensitive growth supports the idea that even modest perturbations of the ATP-driven cycle can propagate to organism-level growth defects. (nadlerholly2012interactionsofsubunit pages 5-6)

4. Beyond cytosolic folding, yeast TRiC has emerging nuclear roles: although the most direct nuclear evidence is not CCT4-specific, the reported RNAPII/RNA-homeostasis role suggests that functional annotation of CCT subunits may increasingly include compartment-specific pools and tasks (possibly via partial complexes or regulated localization). (gvozdenov2024triccctchaperoningoverns pages 21-25)

10) Evidence-backed summary table

Table: This table summarizes the verified identity, complex membership, biochemical role, localization, client proteins, and quantitative data for yeast CCT4/YDL143W/P39078. It is useful as a compact evidence map linking CCT4-specific observations to broader TRiC/CCT literature and recent updates.

11) Key figure evidence for CCT4 ring position (visual citation)

Zang et al. 2018 provides figure-level evidence showing the CCT4-eGFP density and the overall TRiC subunit arrangement with CCT4 assigned as subunit a2. (zang2018developmentofa media f48bc63a, zang2018developmentofa media 2d323812)

12) Limitations of the current evidence base (scope control)

Despite extensive TRiC/CCT literature, yeast CCT4-specific primary experiments that directly identify unique Cct4-only clients (distinct from general TRiC clients) are limited in the retrieved set. The strongest CCT4-specific evidence here is structural position in the ring, allostery-linked mutant phenotypes, quantitative abundance, and cochaperone interaction surfaces; client specificity is best supported at the level of TRiC (actin/tubulin/WD40) with some subunit-resolved contact evidence for tubulin involving CCT4. (zang2018developmentofa pages 3-5, nadlerholly2012interactionsofsubunit pages 5-6, brownridge2013quantitativeanalysisof pages 5-6, shen2025proteinfoldingby pages 1-3)

Selected references (with URLs and publication dates)

• Park J. et al. A structural vista of PhLP2A–TRiC cooperation during the ATP-driven folding cycle. Nature Communications (Feb 2024). https://doi.org/10.1038/s41467-024-45242-x (junsun2024astructuralvista pages 3-4)
• Chen Y. et al. Two distinct regulatory pathways govern Cct2–Atg8 binding in solid aggrephagy. EMBO Reports (Sep 2024). https://doi.org/10.1038/s44319-024-00275-7 (chen2024twodistinctregulatory pages 3-5)
• Gvozdenov Z. et al. TRiC/CCT governs RNA polymerase II activity in the nucleus to support RNA homeostasis. bioRxiv (Sep 2024). https://doi.org/10.1101/2024.09.26.615188 (gvozdenov2024triccctchaperoningoverns pages 21-25)
• Roy M. et al. Reduced ADP off-rate by yeast CCT2 double mutation T394P/R510H (LCA-linked). Communications Biology (Aug 2023). https://doi.org/10.1038/s42003-023-05261-8 (roy2023reducedadpoffrate pages 1-2)
• Que Y. et al. Role of CCT/TRiC in translation elongation (review). Heliyon (Apr 2024). https://doi.org/10.1016/j.heliyon.2024.e29029 (que2024theroleof pages 2-4)
• Zang Y. et al. Yeast internal-subunit eGFP labeling for TRiC subunit identification. Scientific Reports (Feb 2018). https://doi.org/10.1038/s41598-017-18962-y (zang2018developmentofa pages 3-5)
• Willison K.R. Substrate specificity of eukaryotic cytosolic chaperonin CCT (review). Phil. Trans. R. Soc. B (Jun 2018). https://doi.org/10.1098/rstb.2017.0192 (willison2018thesubstratespecificity pages 2-3)
• Brownridge P. et al. Quantitative analysis of chaperone network throughput in budding yeast. Proteomics (Mar 2013). https://doi.org/10.1002/pmic.201200412 (brownridge2013quantitativeanalysisof pages 5-6)
• Nadler-Holly M. et al. CCT3 interactions with Q/N-rich proteins; cites CCT4 allostery mutant phenotype. PNAS (Oct 2012). https://doi.org/10.1073/pnas.1209277109 (nadlerholly2012interactionsofsubunit pages 5-6)
• Shen P.S., Willardson B.M. Protein folding by the CCT/TRiC chaperone complex (review). Current Opinion in Structural Biology (Apr 2025). https://doi.org/10.1016/j.sbi.2025.102999 (shen2025proteinfoldingby pages 1-3)

References

1. (zang2018developmentofa pages 3-5): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.

2. (shen2025proteinfoldingby pages 1-3): Peter S. Shen and Barry M. Willardson. Protein folding by the cct/tric chaperone complex. Current Opinion in Structural Biology, 91:102999, Apr 2025. URL: https://doi.org/10.1016/j.sbi.2025.102999, doi:10.1016/j.sbi.2025.102999. This article has 10 citations and is from a peer-reviewed journal.

3. (que2024theroleof pages 2-4): Yueyue Que, Yudan Qiu, Zheyu Ding, Shanshan Zhang, Rong Wei, Jianing Xia, and Yingying Lin. The role of molecular chaperone cct/tric in translation elongation: a literature review. Heliyon, 10:e29029, Apr 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e29029, doi:10.1016/j.heliyon.2024.e29029. This article has 12 citations.

4. (willison2018thesubstratespecificity pages 1-2): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

5. (dube2021chaperoninpointmutation pages 1-4): Ankita Dube and M. Anaul Kabir. Chaperonin point mutation enhances cadmium endurance in saccharomyces cerevisiae. Biotechnology Letters, 43:1735-1745, May 2021. URL: https://doi.org/10.1007/s10529-021-03151-9, doi:10.1007/s10529-021-03151-9. This article has 2 citations and is from a peer-reviewed journal.

6. (zang2018developmentofa media f48bc63a): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.

7. (zang2018developmentofa media 2d323812): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.

8. (willison2018thesubstratespecificity pages 2-3): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

9. (willison2018thesubstratespecificity pages 6-6): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

10. (nadlerholly2012interactionsofsubunit pages 5-6): Michal Nadler-Holly, Michal Breker, Ranit Gruber, Ariel Azia, Melissa Gymrek, Miriam Eisenstein, Keith R. Willison, Maya Schuldiner, and Amnon Horovitz. Interactions of subunit cct3 in the yeast chaperonin cct/tric with q/n-rich proteins revealed by high-throughput microscopy analysis. Proceedings of the National Academy of Sciences, 109:18833-18838, Oct 2012. URL: https://doi.org/10.1073/pnas.1209277109, doi:10.1073/pnas.1209277109. This article has 52 citations and is from a highest quality peer-reviewed journal.

11. (chen2024twodistinctregulatory pages 3-5): Yuting Chen, Zhaojie Liu, Yi Zhang, Miaojuan Ye, Yingcong Chen, Jianhua Gao, Juan Song, Huan Yang, Choufei Wu, Weijing Yao, Xue Bai, Mingzhu Fan, Shan Feng, Yigang Wang, Liqin Zhang, Liang Ge, Du Feng, and Cong Yi. Two distinct regulatory pathways govern cct2-atg8 binding in the process of solid aggrephagy. EMBO Reports, 25:4749-4776, Sep 2024. URL: https://doi.org/10.1038/s44319-024-00275-7, doi:10.1038/s44319-024-00275-7. This article has 3 citations and is from a highest quality peer-reviewed journal.

12. (willison2018thesubstratespecificity pages 7-8): Keith R. Willison. The substrate specificity of eukaryotic cytosolic chaperonin cct. Philosophical Transactions of the Royal Society B: Biological Sciences, 373:20170192, Jun 2018. URL: https://doi.org/10.1098/rstb.2017.0192, doi:10.1098/rstb.2017.0192. This article has 75 citations and is from a domain leading peer-reviewed journal.

13. (gvozdenov2024triccctchaperoningoverns pages 21-25): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

14. (gvozdenov2024triccctchaperoningoverns pages 30-33): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

15. (nadlerholly2012interactionsofsubunit pages 1-2): Michal Nadler-Holly, Michal Breker, Ranit Gruber, Ariel Azia, Melissa Gymrek, Miriam Eisenstein, Keith R. Willison, Maya Schuldiner, and Amnon Horovitz. Interactions of subunit cct3 in the yeast chaperonin cct/tric with q/n-rich proteins revealed by high-throughput microscopy analysis. Proceedings of the National Academy of Sciences, 109:18833-18838, Oct 2012. URL: https://doi.org/10.1073/pnas.1209277109, doi:10.1073/pnas.1209277109. This article has 52 citations and is from a highest quality peer-reviewed journal.

16. (chen2024twodistinctregulatory pages 5-7): Yuting Chen, Zhaojie Liu, Yi Zhang, Miaojuan Ye, Yingcong Chen, Jianhua Gao, Juan Song, Huan Yang, Choufei Wu, Weijing Yao, Xue Bai, Mingzhu Fan, Shan Feng, Yigang Wang, Liqin Zhang, Liang Ge, Du Feng, and Cong Yi. Two distinct regulatory pathways govern cct2-atg8 binding in the process of solid aggrephagy. EMBO Reports, 25:4749-4776, Sep 2024. URL: https://doi.org/10.1038/s44319-024-00275-7, doi:10.1038/s44319-024-00275-7. This article has 3 citations and is from a highest quality peer-reviewed journal.

17. (brownridge2013quantitativeanalysisof pages 5-6): Philip Brownridge, Craig Lawless, Aishwarya B. Payapilly, Karin Lanthaler, Stephen W. Holman, Victoria M. Harman, Christopher M. Grant, Robert J. Beynon, and Simon J. Hubbard. Quantitative analysis of chaperone network throughput in budding yeast. Proteomics, 13:1276-1291, Mar 2013. URL: https://doi.org/10.1002/pmic.201200412, doi:10.1002/pmic.201200412. This article has 43 citations and is from a peer-reviewed journal.

18. (roy2023reducedadpoffrate pages 1-2): Mousam Roy, Rachel C. Fleisher, Alexander I. Alexandrov, and Amnon Horovitz. Reduced adp off-rate by the yeast cct2 double mutation t394p/r510h which causes leber congenital amaurosis in humans. Communications Biology, Aug 2023. URL: https://doi.org/10.1038/s42003-023-05261-8, doi:10.1038/s42003-023-05261-8. This article has 9 citations and is from a peer-reviewed journal.

19. (junsun2024astructuralvista pages 3-4): Junsun Park, Hyunmin Kim, Daniel Gestaut, Seyeon Lim, Kwadwo A. Opoku-Nsiah, Alexander Leitner, Judith Frydman, and Soung-Hun Roh. A structural vista of phosducin-like phlp2a-chaperonin tric cooperation during the atp-driven folding cycle. Nature Communications, Feb 2024. URL: https://doi.org/10.1038/s41467-024-45242-x, doi:10.1038/s41467-024-45242-x. This article has 16 citations and is from a highest quality peer-reviewed journal.

20. (junsun2024astructuralvista pages 1-2): Junsun Park, Hyunmin Kim, Daniel Gestaut, Seyeon Lim, Kwadwo A. Opoku-Nsiah, Alexander Leitner, Judith Frydman, and Soung-Hun Roh. A structural vista of phosducin-like phlp2a-chaperonin tric cooperation during the atp-driven folding cycle. Nature Communications, Feb 2024. URL: https://doi.org/10.1038/s41467-024-45242-x, doi:10.1038/s41467-024-45242-x. This article has 16 citations and is from a highest quality peer-reviewed journal.

21. (zang2018developmentofa pages 2-3): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.

22. (zang2018developmentofa pages 6-7): Yunxiang Zang, Huping Wang, Zhicheng Cui, Mingliang Jin, Caixuan Liu, Wenyu Han, Yanxing Wang, and Yao Cong. Development of a yeast internal-subunit egfp labeling strategy and its application in subunit identification in eukaryotic group ii chaperonin tric/cct. Scientific Reports, Feb 2018. URL: https://doi.org/10.1038/s41598-017-18962-y, doi:10.1038/s41598-017-18962-y. This article has 22 citations and is from a peer-reviewed journal.

23. (gvozdenov2024triccctchaperoningoverns pages 33-36): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

24. (gvozdenov2024triccctchaperoningoverns pages 25-30): Zlata Gvozdenov, Audrey Yi Tyan Peng, Anusmita Biswas, Zeno Barcutean, Daniel Gestaut, Judith Frydman, Kevin Struhl, and Brian C. Freeman. Tric/cct chaperonin governs rna polymerase ii activity in the nucleus to support rna homeostasis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.26.615188, doi:10.1101/2024.09.26.615188. This article has 3 citations.

Citations

1. zang2018developmentofa pages 3-5
2. shen2025proteinfoldingby pages 1-3
3. willison2018thesubstratespecificity pages 2-3
4. nadlerholly2012interactionsofsubunit pages 5-6
5. chen2024twodistinctregulatory pages 3-5
6. brownridge2013quantitativeanalysisof pages 5-6
7. willison2018thesubstratespecificity pages 7-8
8. willison2018thesubstratespecificity pages 6-6
9. roy2023reducedadpoffrate pages 1-2
10. junsun2024astructuralvista pages 3-4
11. junsun2024astructuralvista pages 1-2
12. gvozdenov2024triccctchaperoningoverns pages 21-25
13. que2024theroleof pages 2-4
14. willison2018thesubstratespecificity pages 1-2
15. dube2021chaperoninpointmutation pages 1-4
16. gvozdenov2024triccctchaperoningoverns pages 30-33
17. nadlerholly2012interactionsofsubunit pages 1-2
18. chen2024twodistinctregulatory pages 5-7
19. zang2018developmentofa pages 2-3
20. zang2018developmentofa pages 6-7
21. gvozdenov2024triccctchaperoningoverns pages 33-36
22. gvozdenov2024triccctchaperoningoverns pages 25-30
23. https://doi.org/10.1016/j.sbi.2025.102999;
24. https://doi.org/10.1016/j.heliyon.2024.e29029
25. https://doi.org/10.1016/j.heliyon.2024.e29029;
26. https://doi.org/10.1007/s10529-021-03151-9
27. https://doi.org/10.1038/s41598-017-18962-y
28. https://doi.org/10.1098/rstb.2017.0192
29. https://doi.org/10.1101/2024.09.26.615188
30. https://doi.org/10.1073/pnas.1209277109;
31. https://doi.org/10.1002/pmic.201200412
32. https://doi.org/10.1101/2024.09.26.615188;
33. https://doi.org/10.1016/j.sbi.2025.102999
34. https://doi.org/10.1038/s41467-024-45242-x
35. https://doi.org/10.1038/s44319-024-00275-7
36. https://doi.org/10.1038/s42003-023-05261-8
37. https://doi.org/10.1073/pnas.1209277109
38. https://doi.org/10.1038/s41598-017-18962-y,
39. https://doi.org/10.1016/j.sbi.2025.102999,
40. https://doi.org/10.1016/j.heliyon.2024.e29029,
41. https://doi.org/10.1098/rstb.2017.0192,
42. https://doi.org/10.1007/s10529-021-03151-9,
43. https://doi.org/10.1073/pnas.1209277109,
44. https://doi.org/10.1038/s44319-024-00275-7,
45. https://doi.org/10.1101/2024.09.26.615188,
46. https://doi.org/10.1002/pmic.201200412,
47. https://doi.org/10.1038/s42003-023-05261-8,
48. https://doi.org/10.1038/s41467-024-45242-x,