ArticleOncotarget
Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins.
Article in Oncotarget. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 39 citations in OpenAlex.
- N-terminal domain of androgen receptor is a major therapeutic barrier and potential pharmacological target for treating castration resistant prostate cancer: a comprehensive review.Frontiers in pharmacology · 2024Review
- Stress Activated MAP Kinases and Cyclin-Dependent Kinase 5 Mediate Nuclear Translocation of Nrf2 via Hsp90α-Pin1-Dynein Motor Transport Machinery.Antioxidants (Basel, Switzerland) · 2023Review
- Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity.Sub-cellular biochemistry · 2023Article
- TTC3-Mediated Protein Quality Control, A Potential Mechanism for Cognitive Impairment.Cellular and molecular neurobiology · 2022Review
- Hsp90 co-chaperones, FKBP52 and Aha1, promote tau pathogenesis in aged wild-type mice.Acta neuropathologica communications · 2021Article
- Article
- Hsp90 Heterocomplexes Regulate Steroid Hormone Receptors: From Stress Response to Psychiatric Disease.International journal of molecular sciences · 2018Review
- Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies.Frontiers in neuroscience · 2017Review
- FKBP14 overexpression contributes to osteosarcoma carcinogenesis and indicates poor survival outcome.Oncotarget · 2016Article
- HSP90AB1: Helping the good and the bad.Gene · 2016Review
- The interchange of immunophilins leads to parallel pathways and different intermediates in the assembly of Hsp90 glucocorticoid receptor complexes.Cell discovery · 2016Article
- Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Nature communications · 2015Article
- pRb controls estrogen receptor alpha protein stability and activity.Oncotarget · 2013Article
- Enzymatic characterization of a lysin encoded by bacteriophage EL.Bacteriophage · 2013Article
- Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.Nature structural & molecular biology · 2013Article
- Serine/threonine protein phosphatase 5 (PP5) interacts with substrate under heat stress conditions and forms protein complex in Arabidopsis.Plant signaling & behavior · 2012Article
- Differential targeting of androgen and glucocorticoid receptors induces ER stress and apoptosis in prostate cancer cells: a novel therapeutic modality.Cell cycle (Georgetown, Tex.) · 2012Article
- FKBP51 and FKBP52 in signaling and disease.Trends in endocrinology and metabolism: TEM · 2011Review
- Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Chaperones and the maturation of steroid hormone receptor complexes.Oncotarget · 2011Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The regulation of steroidogenic hormone receptor-mediated activity plays an important role in the development of hormone-dependent cancers. For example, during prostate carcinogenesis, the regulatory function played by the androgen receptor is often converted from a growth suppressor to an oncogene thus promoting prostate cancer cell survival and eventual metastasis. Within the cytoplasm, steroid hormone receptor activity is regulated by the Hsp90 chaperone in conjunction with a series of co-chaperone proteins. Collectively, Hsp90 and its binding associates form a large heteromeric complex that scaffold the fully mature receptor for binding with the respective hormone. To date our understanding of the interactions between Hsp90 with the various TPR domain-containing co-chaperone proteins is limited due to a lack of available structural information. Here we present the stable formation of Hsp90(2)-FKBP52(1)- HOP(2) and Hsp90(2)-FKBP52(1)-p23(2)-HOP(2) complexes as detected by immunoprecipitation, time course dynamic light scattering and electron microscopy. The simultaneous binding of FKBP52 and HOP to the Hsp90 dimer provide direct evidence of a novel chaperone sub-complex that likely plays a transient role in the regulation of the fully mature steroid hormone receptor.
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What OpenQuestion holds
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.