Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52
Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this cha...
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MDPI AG
2019-02-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/9/2/52 |
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| author | Nadia R. Zgajnar Sonia A. De Leo Cecilia M. Lotufo Alejandra G. Erlejman Graciela Piwien-Pilipuk Mario D. Galigniana |
| author_facet | Nadia R. Zgajnar Sonia A. De Leo Cecilia M. Lotufo Alejandra G. Erlejman Graciela Piwien-Pilipuk Mario D. Galigniana |
| author_sort | Nadia R. Zgajnar |
| collection | DOAJ |
| description | Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects. |
| first_indexed | 2024-12-12T15:40:11Z |
| format | Article |
| id | doaj.art-758520817d9e43e3a1ba8658806280a6 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-12-12T15:40:11Z |
| publishDate | 2019-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-758520817d9e43e3a1ba8658806280a62022-12-22T00:19:55ZengMDPI AGBiomolecules2218-273X2019-02-01925210.3390/biom9020052biom9020052Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52Nadia R. Zgajnar0Sonia A. De Leo1Cecilia M. Lotufo2Alejandra G. Erlejman3Graciela Piwien-Pilipuk4Mario D. Galigniana5Instituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, ArgentinaDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires-CONICET, Buenos Aires 1428, ArgentinaInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, ArgentinaDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires-CONICET, Buenos Aires 1428, ArgentinaInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, ArgentinaInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, ArgentinaImmunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects.https://www.mdpi.com/2218-273X/9/2/52FKBP51FKBP52Hsp90dyneintelomeraseNF-κBneurodifferentiationcell differentiation |
| spellingShingle | Nadia R. Zgajnar Sonia A. De Leo Cecilia M. Lotufo Alejandra G. Erlejman Graciela Piwien-Pilipuk Mario D. Galigniana Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52 Biomolecules FKBP51 FKBP52 Hsp90 dynein telomerase NF-κB neurodifferentiation cell differentiation |
| title | Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52 |
| title_full | Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52 |
| title_fullStr | Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52 |
| title_full_unstemmed | Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52 |
| title_short | Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52 |
| title_sort | biological actions of the hsp90 binding immunophilins fkbp51 and fkbp52 |
| topic | FKBP51 FKBP52 Hsp90 dynein telomerase NF-κB neurodifferentiation cell differentiation |
| url | https://www.mdpi.com/2218-273X/9/2/52 |
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