Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore
In the absence of hormone, corticosteroid receptors such as GR (glucocorticoid receptor) and MR (mineralocorticoid receptor) are primarily located in the cytoplasm. Upon steroid-binding, they rapidly accumulate in the nucleus. Regardless of their primary location, these receptors and many other nucl...
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todo:paper_19491034_v1_n4_p299_Galigniana2023-10-03T16:37:14Z Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore Galigniana, M.D. Echeverría, P.C. Erlejman, A.G. Piwien-Pilipuk, G. Dynein Heat-shock proteins Immunophilins Importins Nucleoporins Shuttling chaperone cyclophilin dynactin fk 506 binding protein glucocorticoid receptor glycoprotein heat shock protein 70 heat shock protein 90 immunoglobulin enhancer binding protein karyopherin beta mineralocorticoid receptor nucleoporin protein nup62 protein p23 serine threonine protein phosphatase 5 tetratricopeptide repeat protein unclassified drug article cell compartmentalization cell nucleus membrane ligand binding nuclear pore complex nucleocytoplasmic transport protein transport signal transduction In the absence of hormone, corticosteroid receptors such as GR (glucocorticoid receptor) and MR (mineralocorticoid receptor) are primarily located in the cytoplasm. Upon steroid-binding, they rapidly accumulate in the nucleus. Regardless of their primary location, these receptors and many other nuclear factors undergo a constant and dynamic nucleocytoplasmic shuttling. All members of the steroid receptor family are known to form large oligomeric structures with the heat-shock proteins of 90-kDa (hsp90) and 70-kDa (hsp70), the small acidic protein p23, and a tetratricopeptide repeat (TPR)-domain protein such as FK506-binding proteins (FKBPs), cyclophilins (CyPs) or the serine/threonine protein phosphatase 5 (PP5). It has always been stated that the dissociation of the chaperone heterocomplex (a process normally referred to as receptor "transformation") is the first step that permits the nuclear import of steroid receptors. However the experimental evidence is consistent with a model where the chaperone machinery is required for the retrotransport of the receptor through the cytoplasm and also facilitates the passage through the nuclear pore. Recent evidence indicates that the hsp90-based chaperone system also interacts with structures of the nuclear pore such as importin β and the integral nuclear pore glycoprotein Nup62 facilitating the passage of the untransformed receptor through the nuclear pore. © 2010 Landes Bioscience. Fil:Echeverría, P.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_19491034_v1_n4_p299_Galigniana |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Dynein Heat-shock proteins Immunophilins Importins Nucleoporins Shuttling chaperone cyclophilin dynactin fk 506 binding protein glucocorticoid receptor glycoprotein heat shock protein 70 heat shock protein 90 immunoglobulin enhancer binding protein karyopherin beta mineralocorticoid receptor nucleoporin protein nup62 protein p23 serine threonine protein phosphatase 5 tetratricopeptide repeat protein unclassified drug article cell compartmentalization cell nucleus membrane ligand binding nuclear pore complex nucleocytoplasmic transport protein transport signal transduction |
| spellingShingle |
Dynein Heat-shock proteins Immunophilins Importins Nucleoporins Shuttling chaperone cyclophilin dynactin fk 506 binding protein glucocorticoid receptor glycoprotein heat shock protein 70 heat shock protein 90 immunoglobulin enhancer binding protein karyopherin beta mineralocorticoid receptor nucleoporin protein nup62 protein p23 serine threonine protein phosphatase 5 tetratricopeptide repeat protein unclassified drug article cell compartmentalization cell nucleus membrane ligand binding nuclear pore complex nucleocytoplasmic transport protein transport signal transduction Galigniana, M.D. Echeverría, P.C. Erlejman, A.G. Piwien-Pilipuk, G. Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore |
| topic_facet |
Dynein Heat-shock proteins Immunophilins Importins Nucleoporins Shuttling chaperone cyclophilin dynactin fk 506 binding protein glucocorticoid receptor glycoprotein heat shock protein 70 heat shock protein 90 immunoglobulin enhancer binding protein karyopherin beta mineralocorticoid receptor nucleoporin protein nup62 protein p23 serine threonine protein phosphatase 5 tetratricopeptide repeat protein unclassified drug article cell compartmentalization cell nucleus membrane ligand binding nuclear pore complex nucleocytoplasmic transport protein transport signal transduction |
| description |
In the absence of hormone, corticosteroid receptors such as GR (glucocorticoid receptor) and MR (mineralocorticoid receptor) are primarily located in the cytoplasm. Upon steroid-binding, they rapidly accumulate in the nucleus. Regardless of their primary location, these receptors and many other nuclear factors undergo a constant and dynamic nucleocytoplasmic shuttling. All members of the steroid receptor family are known to form large oligomeric structures with the heat-shock proteins of 90-kDa (hsp90) and 70-kDa (hsp70), the small acidic protein p23, and a tetratricopeptide repeat (TPR)-domain protein such as FK506-binding proteins (FKBPs), cyclophilins (CyPs) or the serine/threonine protein phosphatase 5 (PP5). It has always been stated that the dissociation of the chaperone heterocomplex (a process normally referred to as receptor "transformation") is the first step that permits the nuclear import of steroid receptors. However the experimental evidence is consistent with a model where the chaperone machinery is required for the retrotransport of the receptor through the cytoplasm and also facilitates the passage through the nuclear pore. Recent evidence indicates that the hsp90-based chaperone system also interacts with structures of the nuclear pore such as importin β and the integral nuclear pore glycoprotein Nup62 facilitating the passage of the untransformed receptor through the nuclear pore. © 2010 Landes Bioscience. |
| format |
JOUR |
| author |
Galigniana, M.D. Echeverría, P.C. Erlejman, A.G. Piwien-Pilipuk, G. |
| author_facet |
Galigniana, M.D. Echeverría, P.C. Erlejman, A.G. Piwien-Pilipuk, G. |
| author_sort |
Galigniana, M.D. |
| title |
Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore |
| title_short |
Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore |
| title_full |
Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore |
| title_fullStr |
Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore |
| title_full_unstemmed |
Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore |
| title_sort |
role of molecular chaperones and tpr-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore |
| url |
http://hdl.handle.net/20.500.12110/paper_19491034_v1_n4_p299_Galigniana |
| work_keys_str_mv |
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