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Functions of the Hsp90-binding FKBP immunophilins.
Subcell Biochem. 2015; 78:35-68.SB

Abstract

Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members.

Authors+Show Affiliations

Department of Biological Sciences, Border Biomedical Research Center, University of Texas at El Paso, 79968, El Paso, TX, USA, ncguy@utep.edu.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

25487015

Citation

Guy, Naihsuan C., et al. "Functions of the Hsp90-binding FKBP Immunophilins." Sub-cellular Biochemistry, vol. 78, 2015, pp. 35-68.
Guy NC, Garcia YA, Sivils JC, et al. Functions of the Hsp90-binding FKBP immunophilins. Subcell Biochem. 2015;78:35-68.
Guy, N. C., Garcia, Y. A., Sivils, J. C., Galigniana, M. D., & Cox, M. B. (2015). Functions of the Hsp90-binding FKBP immunophilins. Sub-cellular Biochemistry, 78, 35-68. https://doi.org/10.1007/978-3-319-11731-7_2
Guy NC, et al. Functions of the Hsp90-binding FKBP Immunophilins. Subcell Biochem. 2015;78:35-68. PubMed PMID: 25487015.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Functions of the Hsp90-binding FKBP immunophilins. AU - Guy,Naihsuan C, AU - Garcia,Yenni A, AU - Sivils,Jeffrey C, AU - Galigniana,Mario D, AU - Cox,Marc B, PY - 2014/12/10/entrez PY - 2014/12/10/pubmed PY - 2015/5/1/medline SP - 35 EP - 68 JF - Sub-cellular biochemistry JO - Subcell Biochem VL - 78 N2 - Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members. SN - 0306-0225 UR - https://www.unboundmedicine.com/medline/citation/25487015/Functions_of_the_Hsp90_binding_FKBP_immunophilins_ L2 - https://dx.doi.org/10.1007/978-3-319-11731-7_2 DB - PRIME DP - Unbound Medicine ER -