ArticleThe Journal of biological chemistry2011
Prefoldin subunits are protected from ubiquitin-proteasome system-mediated degradation by forming complex with other constituent subunits.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Prefoldin Subunit 2 Promotes Migration of Hepatocellular Carcinoma Cells and Is Associated with Poor Prognosis.Annals of surgical oncology · 2026Article
- Prefoldin 3 promotes the turnover of WRKY70 and FHY3 to modulate UV-B-induced hypocotyl growth inhibition in Arabidopsis thaliana.Plant communications · 2026Article
- Article
- A distinct P-body-like granule is induced in response to the disruption of microtubule integrity in Saccharomyces cerevisiae.Genetics · 2022Article
- Review
- Human prefoldin modulates co-transcriptional pre-mRNA splicing.Nucleic acids research · 2021Article
- The prefoldin complex stabilizes the von Hippel-Lindau protein against aggregation and degradation.PLoS genetics · 2020Article
- The functions and mechanisms of prefoldin complex and prefoldin-subunits.Cell & bioscience · 2020Review
- The Role of Prefoldin and Its Subunits in Tumors and Their Application Prospects in Nanomedicine.Cancer management and research · 2020Review
- Colorectal cancer cells display chaperone dependency for the unconventional prefoldin URI1.Oncotarget · 2016Article
- PFDN1, an indicator for colorectal cancer prognosis, enhances tumor cell proliferation and motility through cytoskeletal reorganization.Medical oncology (Northwood, London, England) · 2015Article
- VBP1 facilitates proteasome and autophagy-mediated degradation of MutS homologue hMSH4.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- Prefoldin plays a role as a clearance factor in preventing proteasome inhibitor-induced protein aggregation.The Journal of biological chemistry · 2013Article
- Prefoldin protects neuronal cells from polyglutamine toxicity by preventing aggregation formation.The Journal of biological chemistry · 2013Article
- The prefoldin bud27 mediates the assembly of the eukaryotic RNA polymerases in an rpb5-dependent manner.PLoS genetics · 2013Article
- Genome evolution in the cold: Antarctic icefish muscle transcriptome reveals selective duplications increasing mitochondrial function.Genome biology and evolution · 2013Article
- The role of 26S proteasome-dependent proteolysis in the formation and restructuring of microtubule networks.Plant signaling & behavior · 2012Review
- Rabring7 degrades c-Myc through complex formation with MM-1.PloS one · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular chaperone prefoldin (PFD) is a complex comprised of six different subunits, PFD1-PFD6, and delivers newly synthesized unfolded proteins to cytosolic chaperonin TRiC/CCT to facilitate the folding of proteins. PFD subunits also have functions different from the function of the PFD complex. We previously identified MM-1α/PFD5 as a novel c-Myc-binding protein and found that MM-1α suppresses transformation activity of c-Myc. However, it remains unclear how cells regulate protein levels of individual subunits and what mechanisms alter the ratio of their activities between subunits and their complex. In this study, we found that knockdown of one subunit decreased protein levels of other subunits and that transfection of five subunits other than MM-1α into cells increased the level of endogenous MM-1α. We also found that treatment of cells with MG132, a proteasome inhibitor, increased the level of transfected/overexpressed MM-1α but not that of endogenous MM-1α, indicating that overexpressed MM-1α, but not endogenous MM-1α, was degraded by the ubiquitin proteasome system (UPS). Experiments using other PFD subunits showed that the UPS degraded a monomer of PFD subunits, though extents of degradation varied among subunits. Furthermore, the level of one subunit was increased after co-transfection with the respective subunit, indicating that there are specific combinations between subunits to be stabilized. These results suggest mutual regulation of protein levels among PFD subunits and show how individual subunits form the PFD complex without degradation.
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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.