ArticleThe EMBO journal2012
The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
121 citing papers in PubMed, 225 citations in OpenAlex.
- Dynamic global acetylation remodeling during the yeast heat shock response.Genome biology · 2026Article
- Hsp90: A means to an end.Cell stress & chaperones · 2026Review
- De-repression of protein phosphatase 5 by the chaperone organizer HOP1 activates plant NLR immunity.Nature plants · 2026Article
- STI1 domain engages transient helices to mediate Dsk2 phase separation and proteasome condensation.The EMBO journal · 2026Article
- Emw1/TTC27 is a chaperone required for folding of the eukaryotic elongation factor 2.Cellular and molecular life sciences : CMLS · 2026Article
- Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026Review
- Hsp90 and associates shaping parasite biology.mSphere · 2025Review
- Article
- PGRP-S promotes hepatocellular carcinoma progression via MAPK/ERK pathway by interaction with TTC1.Scientific reports · 2025Article
- Stress-inducible phosphoprotein 1 (Sti1/Stip1/Hop) sequesters misfolded proteins during stress.The FEBS journal · 2025Article
- Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins.Trends in biochemical sciences · 2025Review
- Interactome screening implicates BAG6 as a suppressor of UBQLN2 misfolding in ALS/FTD.Frontiers in molecular neuroscience · 2025Article
- Co-chaperones fine-tune the function of heat shock protein 70 (Hsp70), whether to fold, hold, or degrade substrates in ensuring cellular protein homeostasis.Journal of biosciences · 2025Review
- Insights into the Allosteric Regulation of Human Hsp90 Revealed by NMR Spectroscopy.Biomolecules · 2024Review
- The role of the co-chaperone HOP in plant homeostasis during development and stress.Journal of experimental botany · 2024Review
- Strategies that regulate LSD1 for novel therapeutics.Acta pharmaceutica Sinica. B · 2024Review
- Structural and functional complexity of HSP90 in cellular homeostasis and disease.Nature reviews. Molecular cell biology · 2023Review
- [STIP1 correlates with tumor immune infiltration and prognosis as a potential immunotherapy target: a pan-cancer bioinformatics analysis].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2023Article
- Article
- Detecting Posttranslational Modifications of Hsp90 Isoforms.Methods in molecular biology (Clifton, N.J.) · 2023Article
61 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Sti1/Hop is a modular protein required for the transfer of client proteins from the Hsp70 to the Hsp90 chaperone system in eukaryotes. It binds Hsp70 and Hsp90 simultaneously via TPR (tetratricopeptide repeat) domains. Sti1/Hop contains three TPR domains (TPR1, TPR2A and TPR2B) and two domains of unknown structure (DP1 and DP2). We show that TPR2A is the high affinity Hsp90-binding site and TPR1 and TPR2B bind Hsp70 with moderate affinity. The DP domains exhibit highly homologous α-helical folds as determined by NMR. These, and especially DP2, are important for client activation in vivo. The core module of Sti1 for Hsp90 inhibition is the TPR2A-TPR2B segment. In the crystal structure, the two TPR domains are connected via a rigid linker orienting their peptide-binding sites in opposite directions and allowing the simultaneous binding of TPR2A to the Hsp90 C-terminal domain and of TPR2B to Hsp70. Both domains also interact with the Hsp90 middle domain. The accessory TPR1-DP1 module may serve as an Hsp70-client delivery system for the TPR2A-TPR2B-DP2 segment, which is required for client activation in vivo.
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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.