ArticleMolecular biology of the cell2008
Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 58 citations in OpenAlex.
- Cdc42 interacts with chaperone Ydj1 to enhance its stability and partitioning during asymmetric cell division and aging in yeast.PLoS biology · 2026Article
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.PLoS genetics · 2024Article
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.bioRxiv : the preprint server for biology · 2024Article
- Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones.Cell stress & chaperones · 2024Review
- Activation of autophagy depends on Atg1/Ulk1-mediated phosphorylation and inhibition of the Hsp90 chaperone machinery.Cell reports · 2023Article
- Analysis of the Interactome of theProteomes · 2023Article
- Functional classification and validation of yeast prenylation motifs using machine learning and genetic reporters.PloS one · 2022Article
- Protein Prenylation and Hsp40 in Thermotolerance of Plasmodium falciparum Malaria Parasites.mBio · 2021Article
- Role of the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum.Advances in experimental medicine and biology · 2021Review
- Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling.The Journal of biological chemistry · 2019Review
- Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90.Cell reports · 2019Article
- The Farnesyltransferase β-Subunit Ram1 RegulatesFrontiers in microbiology · 2019Article
- Protein Isoprenylation in Yeast Targets COOH-Terminal Sequences Not Adhering to the CaaX Consensus.Genetics · 2018Article
- The Hsp70 co-chaperone Ydj1/HDJ2 regulates ribonucleotide reductase activity.PLoS genetics · 2018Article
- Farnesylated heat shock protein 40 is a component of membrane-bound RISC inThe Journal of biological chemistry · 2018Article
- Functional and physical interaction between yeast Hsp90 and Hsp70.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Heat-shock protein 40 is the key farnesylation target in meristem size control, abscisic acid signaling, and drought resistance.Genes & development · 2017Article
- An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.Nature communications · 2017Article
- Hsp70/J-protein machinery from Glossina morsitans morsitans, vector of African trypanosomiasis.PloS one · 2017Article
- Global proteomic analysis of prenylated proteins in Plasmodium falciparum using an alkyne-modified isoprenoid analogue.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ydj1 of Saccharomyces cerevisiae is an abundant cytosolic Hsp40, or J-type, molecular chaperone. Ydj1 cooperates with Hsp70 of the Ssa family in the translocation of preproteins to the ER and mitochondria and in the maturation of Hsp90 client proteins. The substrate-binding domain of Ydj1 directly interacts with steroid receptors and is required for the activity of diverse Hsp90-dependent client proteins. However, the effect of Ydj1 alteration on client interaction was unknown. We analyzed the in vivo interaction of Ydj1 with the protein kinase Ste11 and the glucocorticoid receptor. Amino acid alterations in the proposed client-binding domain or zinc-binding domain had minor effects on the physical interaction of Ydj1 with both clients. However, alteration of the carboxy-terminal farnesylation signal disrupted the functional and physical interaction of Ydj1 and Hsp90 with both clients. Similar effects were observed upon deletion of RAM1, which encodes one of the subunits of yeast farnesyltransferase. Our results indicate that farnesylation is a major factor contributing to the specific requirement for Ydj1 in promoting proper regulation and activation of diverse Hsp90 clients.
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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.