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S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats.
FEBS Lett. 2010 Mar 19; 584(6):1119-25.FL

Abstract

S100 proteins are a subfamily of the EF-hand type calcium sensing proteins, the exact biological functions of which have not been clarified yet. In this work, we have identified Cyclophilin 40 (CyP40) and FKBP52 (called immunophilins) as novel targets of S100 proteins. These immunophilins contain a tetratricopeptide repeat (TPR) domain for Hsp90 binding. Using glutathione-S transferase pull-down assays and immunoprecipitation, we have demonstrated that S100A1 and S100A2 specifically interact with the TPR domains of FKBP52 and CyP40 in a Ca(2+)-dependent manner, and lead to inhibition of the CyP40-Hsp90 and FKBP52-Hsp90 interactions. These findings have suggested that the Ca(2+)/S100 proteins are TPR-targeting regulators of the immunophilins-Hsp90 complex formations.

Authors+Show Affiliations

Department of Signal Transduction Sciences, Kagawa University Faculty of Medicine, Kita-gun, Kagawa, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20188096

Citation

Shimamoto, Seiko, et al. "S100 Proteins Regulate the Interaction of Hsp90 With Cyclophilin 40 and FKBP52 Through Their Tetratricopeptide Repeats." FEBS Letters, vol. 584, no. 6, 2010, pp. 1119-25.
Shimamoto S, Kubota Y, Tokumitsu H, et al. S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats. FEBS Lett. 2010;584(6):1119-25.
Shimamoto, S., Kubota, Y., Tokumitsu, H., & Kobayashi, R. (2010). S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats. FEBS Letters, 584(6), 1119-25. https://doi.org/10.1016/j.febslet.2010.02.055
Shimamoto S, et al. S100 Proteins Regulate the Interaction of Hsp90 With Cyclophilin 40 and FKBP52 Through Their Tetratricopeptide Repeats. FEBS Lett. 2010 Mar 19;584(6):1119-25. PubMed PMID: 20188096.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats. AU - Shimamoto,Seiko, AU - Kubota,Yasuo, AU - Tokumitsu,Hiroshi, AU - Kobayashi,Ryoji, Y1 - 2010/02/24/ PY - 2009/12/15/received PY - 2010/01/30/revised PY - 2010/02/15/accepted PY - 2010/3/2/entrez PY - 2010/3/2/pubmed PY - 2010/4/27/medline SP - 1119 EP - 25 JF - FEBS letters JO - FEBS Lett VL - 584 IS - 6 N2 - S100 proteins are a subfamily of the EF-hand type calcium sensing proteins, the exact biological functions of which have not been clarified yet. In this work, we have identified Cyclophilin 40 (CyP40) and FKBP52 (called immunophilins) as novel targets of S100 proteins. These immunophilins contain a tetratricopeptide repeat (TPR) domain for Hsp90 binding. Using glutathione-S transferase pull-down assays and immunoprecipitation, we have demonstrated that S100A1 and S100A2 specifically interact with the TPR domains of FKBP52 and CyP40 in a Ca(2+)-dependent manner, and lead to inhibition of the CyP40-Hsp90 and FKBP52-Hsp90 interactions. These findings have suggested that the Ca(2+)/S100 proteins are TPR-targeting regulators of the immunophilins-Hsp90 complex formations. SN - 1873-3468 UR - https://www.unboundmedicine.com/medline/citation/20188096/S100_proteins_regulate_the_interaction_of_Hsp90_with_Cyclophilin_40_and_FKBP52_through_their_tetratricopeptide_repeats_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-5793(10)00159-6 DB - PRIME DP - Unbound Medicine ER -