Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52
Immunophilins comprise a family of intracellular proteins with peptidyl-prolyl-(cis/trans)-isomerase activity. These foldases are abundant, ubiquitous, and able to bind immunosuppressant drugs, from which the term immunophilin derives. Family members are found in abundance in virtually all organisms...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_13892037_v15_n3_p205_Erlejman |
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todo:paper_13892037_v15_n3_p205_Erlejman2023-10-03T16:12:43Z Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 Erlejman, A.G. Lagadari, M. Harris, D.C. Cox, M.B. Galigniana, M.D. FK506 FKBP51 FKBP52 Hsp70 Hsp90 Immunophilin Peptidylprolyl isomerase TPR chaperone cyclosporin A fk 506 binding protein heat shock protein 90 immunophilin peptidylprolyl isomerase proline rich protein protein FKB52 protein FKBP51 protein S 100 rapamycin tacrolimus tau protein unclassified drug chaperone fk 506 binding protein steroid receptor tacrolimus binding protein 4 tacrolimus binding protein 5 Alzheimer disease article breast cancer cell growth cell proliferation complex formation cytoskeleton gene expression gene overexpression human nerve cell differentiation nonhuman ovary cancer protein assembly protein binding protein domain protein expression protein function protein interaction protein localization protein phosphorylation tetratricopeptide repeat chemistry metabolism protein folding protein tertiary structure Humans Molecular Chaperones Protein Folding Protein Structure, Tertiary Receptors, Steroid Tacrolimus Binding Proteins Immunophilins comprise a family of intracellular proteins with peptidyl-prolyl-(cis/trans)-isomerase activity. These foldases are abundant, ubiquitous, and able to bind immunosuppressant drugs, from which the term immunophilin derives. Family members are found in abundance in virtually all organisms and subcellular compartments, and their amino acid sequences are conserved phylogenetically. Immunophilins possess the ability to function as molecular chaperones favoring the proper folding and biological regulation of their biological actions. Their ability to interact via their TPR domains with the 90-kDa heat-shock protein, and through this chaperone, with several signalling cascade factors is of particular importance. Among the family members, the highly homologous proteins FKBP51 and FKBP52 were first characterized due to their ability to interact with steroid hormone receptors. Since then, much progress has been made in understanding the mechanisms by which they regulate receptor signaling and the resulting roles they play not only in endocrine processes, but also in cell architecture, neurodifferentiation, and tumor progression. In this article we review the most relevant features of these two immunophilins and their potential as pharmacologic targets. © 2014 Bentham Science Publishers. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13892037_v15_n3_p205_Erlejman |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
FK506 FKBP51 FKBP52 Hsp70 Hsp90 Immunophilin Peptidylprolyl isomerase TPR chaperone cyclosporin A fk 506 binding protein heat shock protein 90 immunophilin peptidylprolyl isomerase proline rich protein protein FKB52 protein FKBP51 protein S 100 rapamycin tacrolimus tau protein unclassified drug chaperone fk 506 binding protein steroid receptor tacrolimus binding protein 4 tacrolimus binding protein 5 Alzheimer disease article breast cancer cell growth cell proliferation complex formation cytoskeleton gene expression gene overexpression human nerve cell differentiation nonhuman ovary cancer protein assembly protein binding protein domain protein expression protein function protein interaction protein localization protein phosphorylation tetratricopeptide repeat chemistry metabolism protein folding protein tertiary structure Humans Molecular Chaperones Protein Folding Protein Structure, Tertiary Receptors, Steroid Tacrolimus Binding Proteins |
| spellingShingle |
FK506 FKBP51 FKBP52 Hsp70 Hsp90 Immunophilin Peptidylprolyl isomerase TPR chaperone cyclosporin A fk 506 binding protein heat shock protein 90 immunophilin peptidylprolyl isomerase proline rich protein protein FKB52 protein FKBP51 protein S 100 rapamycin tacrolimus tau protein unclassified drug chaperone fk 506 binding protein steroid receptor tacrolimus binding protein 4 tacrolimus binding protein 5 Alzheimer disease article breast cancer cell growth cell proliferation complex formation cytoskeleton gene expression gene overexpression human nerve cell differentiation nonhuman ovary cancer protein assembly protein binding protein domain protein expression protein function protein interaction protein localization protein phosphorylation tetratricopeptide repeat chemistry metabolism protein folding protein tertiary structure Humans Molecular Chaperones Protein Folding Protein Structure, Tertiary Receptors, Steroid Tacrolimus Binding Proteins Erlejman, A.G. Lagadari, M. Harris, D.C. Cox, M.B. Galigniana, M.D. Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 |
| topic_facet |
FK506 FKBP51 FKBP52 Hsp70 Hsp90 Immunophilin Peptidylprolyl isomerase TPR chaperone cyclosporin A fk 506 binding protein heat shock protein 90 immunophilin peptidylprolyl isomerase proline rich protein protein FKB52 protein FKBP51 protein S 100 rapamycin tacrolimus tau protein unclassified drug chaperone fk 506 binding protein steroid receptor tacrolimus binding protein 4 tacrolimus binding protein 5 Alzheimer disease article breast cancer cell growth cell proliferation complex formation cytoskeleton gene expression gene overexpression human nerve cell differentiation nonhuman ovary cancer protein assembly protein binding protein domain protein expression protein function protein interaction protein localization protein phosphorylation tetratricopeptide repeat chemistry metabolism protein folding protein tertiary structure Humans Molecular Chaperones Protein Folding Protein Structure, Tertiary Receptors, Steroid Tacrolimus Binding Proteins |
| description |
Immunophilins comprise a family of intracellular proteins with peptidyl-prolyl-(cis/trans)-isomerase activity. These foldases are abundant, ubiquitous, and able to bind immunosuppressant drugs, from which the term immunophilin derives. Family members are found in abundance in virtually all organisms and subcellular compartments, and their amino acid sequences are conserved phylogenetically. Immunophilins possess the ability to function as molecular chaperones favoring the proper folding and biological regulation of their biological actions. Their ability to interact via their TPR domains with the 90-kDa heat-shock protein, and through this chaperone, with several signalling cascade factors is of particular importance. Among the family members, the highly homologous proteins FKBP51 and FKBP52 were first characterized due to their ability to interact with steroid hormone receptors. Since then, much progress has been made in understanding the mechanisms by which they regulate receptor signaling and the resulting roles they play not only in endocrine processes, but also in cell architecture, neurodifferentiation, and tumor progression. In this article we review the most relevant features of these two immunophilins and their potential as pharmacologic targets. © 2014 Bentham Science Publishers. |
| format |
JOUR |
| author |
Erlejman, A.G. Lagadari, M. Harris, D.C. Cox, M.B. Galigniana, M.D. |
| author_facet |
Erlejman, A.G. Lagadari, M. Harris, D.C. Cox, M.B. Galigniana, M.D. |
| author_sort |
Erlejman, A.G. |
| title |
Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 |
| title_short |
Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 |
| title_full |
Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 |
| title_fullStr |
Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 |
| title_full_unstemmed |
Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52 |
| title_sort |
molecular chaperone activity and biological regulatory actions of the tpr-domain immunophilins fkbp51 and fkbp52 |
| url |
http://hdl.handle.net/20.500.12110/paper_13892037_v15_n3_p205_Erlejman |
| work_keys_str_mv |
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| _version_ |
1782029800304541696 |