ArticlePloS one2008
The human TPR protein TTC4 is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
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- Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins.Trends in biochemical sciences · 2025Review
- Hsp90: From Cellular to Organismal Proteostasis.Cells · 2022Review
- Hsp90 and Associated Co-Chaperones of the Malaria Parasite.Biomolecules · 2022Review
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- Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions.Cell stress & chaperones · 2021Review
- Tetratricopeptide repeat domain 7A is a nuclear factor that modulates transcription and chromatin structure.Cell discovery · 2018Article
- Characterization of tetratricopeptide repeat-containing proteins critical for cilia formation and function.PloS one · 2015Article
- The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome.Eukaryotic cell · 2015Article
- Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.Current genetics · 2014Article
- Molecular cochaperones: tumor growth and cancer treatment.Scientifica · 2013Review
- Novel Hsp90 partners discovered using complementary proteomic approaches.Cell stress & chaperones · 2009Article
- Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.Cell stress & chaperones · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe human TTC4 protein is a TPR (tetratricopeptide repeat) motif-containing protein. The gene was originally identified as being localized in a genomic region linked to breast cancer and subsequent studies on melanoma cell lines revealed point mutations in the TTC4 protein that may be associated with the progression of malignant melanoma. METHODOLOGY/PRINCIPLE
findingsHere we show that TTC4 is a nucleoplasmic protein which interacts with HSP90 and HSP70, and also with the replication protein CDC6. It has significant structural and functional similarities with a previously characterised Drosophila protein Dpit47. We show that TTC4 protein levels are raised in malignant melanoma cell lines compared to melanocytes. We also see increased TTC4 expression in a variety of tumour lines derived from other tissues. In addition we show that TTC4 proteins bearing some of the mutations previously identified from patient samples lose their interaction with the CDC6 protein. CONCLUSIONS/SIGNIFICANCE: Based on these results and our previous work with the Drosophila Dpit47 protein we suggest that TTC4 is an HSP90 co-chaperone protein which forms a link between HSP90 chaperone activity and DNA replication. We further suggest that the loss of the interaction with CDC6 or with additional client proteins could provide one route through which TTC4 could influence malignant development of cells.
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