Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex

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Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known. In contrast, the high molecular weight hsp90-binding immunophilins appear to pl...

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Autores principales:	Galigniana, M.D., Morishima, Y., Gallay, P.A., Pratt, W.B.
Formato:	Artículo publishedVersion
Lenguaje:	Inglés
Publicado:	2004
Materias:	Cells Cytology Drug products Immunology Living systems studies Molecular weight Immunophilins Microtubules Prolyl isomerase Protein trafficking Proteins cyclophilin cyclophilin A cyclosporin A dynein adenosine triphosphatase heat shock protein 90 immunophilin immunosuppressive agent protein p53 tubulin animal cell article complex formation controlled study cytoplasm cytosol enzyme activity in vitro study in vivo study microtubule molecular weight mouse nonhuman priority journal protein binding protein domain protein expression protein function protein localization protein protein interaction protein synthesis protein transport Animals Cell Line Cell-Free System Cyclophilin A Cyclosporine Cytoplasm Fluorescent Antibody Technique, Indirect Glutathione HSP90 Heat-Shock Proteins Immunoblotting Immunosuppressive Agents Mice Microtubule-Associated Proteins NIH 3T3 Cells Peptidylprolyl Isomerase Plasmids Protein Binding Protein Structure, Tertiary Rabbits Receptors, Glucocorticoid Tumor Suppressor Protein p53 Animalia Mammalia
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00219258_v279_n53_p55754_Galigniana
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paperaa:paper_00219258_v279_n53_p55754_Galigniana
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spelling	paperaa:paper_00219258_v279_n53_p55754_Galigniana2023-06-12T16:42:53Z Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex J. Biol. Chem. 2004;279(53):55754-55759 Galigniana, M.D. Morishima, Y. Gallay, P.A. Pratt, W.B. Cells Cytology Drug products Immunology Living systems studies Molecular weight Immunophilins Microtubules Prolyl isomerase Protein trafficking Proteins cyclophilin cyclophilin A cyclosporin A dynein adenosine triphosphatase heat shock protein 90 immunophilin immunosuppressive agent protein p53 tubulin animal cell article complex formation controlled study cytoplasm cytosol enzyme activity in vitro study in vivo study microtubule molecular weight mouse nonhuman priority journal protein binding protein domain protein expression protein function protein localization protein protein interaction protein synthesis protein transport Animals Cell Line Cell-Free System Cyclophilin A Cyclosporine Cytoplasm Fluorescent Antibody Technique, Indirect Glutathione HSP90 Heat-Shock Proteins Immunoblotting Immunosuppressive Agents Mice Microtubule-Associated Proteins Microtubules NIH 3T3 Cells Peptidylprolyl Isomerase Plasmids Protein Binding Protein Structure, Tertiary Rabbits Receptors, Glucocorticoid Tumor Suppressor Protein p53 Animalia Mammalia Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known. In contrast, the high molecular weight hsp90-binding immunophilins appear to play a role in protein trafficking in that they have been shown to link glucocorticoid receptor-hsp90 and p53-hsp90 complexes to the dynein motor protein for retrograde movement along microtubules. These immunophilins link to cytoplasmic dynein indirectly through the association of the immunophilin peptidylprolyl isomerase (PPIase) domain with dynamitin, a component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Here, we show that CyP-A exists in native heterocomplexes containing cytoplasmic dynein that can be formed in cell-free systems. Prolyl isomerase activity is not required for forming the dynein complex, but the PPIase domain fragment of FKBP52 blocks complex formation and CyP-A binds to dynamitin in a PPIase domain-dependent manner. CyP-A heterocomplexes containing tubulin and dynein can be formed in cytosol prepared under microtubule-stabilizing conditions, and CyP-A colocalizes in mouse fibroblasts with microtubules. Colocalization with microtubules is disrupted by overexpression of the PPIase domain fragment. Thus, we conclude that CyP-A associates in vitro and in vivo with the dynein/dynactin motor protein complex and we suggest that CyP-A may perform a general function related to the binding of cargo for retrograde movement along microtubules. 2004 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219258_v279_n53_p55754_Galigniana
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language	Inglés
orig_language_str_mv	eng
topic	Cells Cytology Drug products Immunology Living systems studies Molecular weight Immunophilins Microtubules Prolyl isomerase Protein trafficking Proteins cyclophilin cyclophilin A cyclosporin A dynein adenosine triphosphatase heat shock protein 90 immunophilin immunosuppressive agent protein p53 tubulin animal cell article complex formation controlled study cytoplasm cytosol enzyme activity in vitro study in vivo study microtubule molecular weight mouse nonhuman priority journal protein binding protein domain protein expression protein function protein localization protein protein interaction protein synthesis protein transport Animals Cell Line Cell-Free System Cyclophilin A Cyclosporine Cytoplasm Fluorescent Antibody Technique, Indirect Glutathione HSP90 Heat-Shock Proteins Immunoblotting Immunosuppressive Agents Mice Microtubule-Associated Proteins Microtubules NIH 3T3 Cells Peptidylprolyl Isomerase Plasmids Protein Binding Protein Structure, Tertiary Rabbits Receptors, Glucocorticoid Tumor Suppressor Protein p53 Animalia Mammalia
spellingShingle	Cells Cytology Drug products Immunology Living systems studies Molecular weight Immunophilins Microtubules Prolyl isomerase Protein trafficking Proteins cyclophilin cyclophilin A cyclosporin A dynein adenosine triphosphatase heat shock protein 90 immunophilin immunosuppressive agent protein p53 tubulin animal cell article complex formation controlled study cytoplasm cytosol enzyme activity in vitro study in vivo study microtubule molecular weight mouse nonhuman priority journal protein binding protein domain protein expression protein function protein localization protein protein interaction protein synthesis protein transport Animals Cell Line Cell-Free System Cyclophilin A Cyclosporine Cytoplasm Fluorescent Antibody Technique, Indirect Glutathione HSP90 Heat-Shock Proteins Immunoblotting Immunosuppressive Agents Mice Microtubule-Associated Proteins Microtubules NIH 3T3 Cells Peptidylprolyl Isomerase Plasmids Protein Binding Protein Structure, Tertiary Rabbits Receptors, Glucocorticoid Tumor Suppressor Protein p53 Animalia Mammalia Galigniana, M.D. Morishima, Y. Gallay, P.A. Pratt, W.B. Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
topic_facet	Cells Cytology Drug products Immunology Living systems studies Molecular weight Immunophilins Microtubules Prolyl isomerase Protein trafficking Proteins cyclophilin cyclophilin A cyclosporin A dynein adenosine triphosphatase heat shock protein 90 immunophilin immunosuppressive agent protein p53 tubulin animal cell article complex formation controlled study cytoplasm cytosol enzyme activity in vitro study in vivo study microtubule molecular weight mouse nonhuman priority journal protein binding protein domain protein expression protein function protein localization protein protein interaction protein synthesis protein transport Animals Cell Line Cell-Free System Cyclophilin A Cyclosporine Cytoplasm Fluorescent Antibody Technique, Indirect Glutathione HSP90 Heat-Shock Proteins Immunoblotting Immunosuppressive Agents Mice Microtubule-Associated Proteins Microtubules NIH 3T3 Cells Peptidylprolyl Isomerase Plasmids Protein Binding Protein Structure, Tertiary Rabbits Receptors, Glucocorticoid Tumor Suppressor Protein p53 Animalia Mammalia
description	Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known. In contrast, the high molecular weight hsp90-binding immunophilins appear to play a role in protein trafficking in that they have been shown to link glucocorticoid receptor-hsp90 and p53-hsp90 complexes to the dynein motor protein for retrograde movement along microtubules. These immunophilins link to cytoplasmic dynein indirectly through the association of the immunophilin peptidylprolyl isomerase (PPIase) domain with dynamitin, a component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Here, we show that CyP-A exists in native heterocomplexes containing cytoplasmic dynein that can be formed in cell-free systems. Prolyl isomerase activity is not required for forming the dynein complex, but the PPIase domain fragment of FKBP52 blocks complex formation and CyP-A binds to dynamitin in a PPIase domain-dependent manner. CyP-A heterocomplexes containing tubulin and dynein can be formed in cytosol prepared under microtubule-stabilizing conditions, and CyP-A colocalizes in mouse fibroblasts with microtubules. Colocalization with microtubules is disrupted by overexpression of the PPIase domain fragment. Thus, we conclude that CyP-A associates in vitro and in vivo with the dynein/dynactin motor protein complex and we suggest that CyP-A may perform a general function related to the binding of cargo for retrograde movement along microtubules.
format	Artículo Artículo publishedVersion
author	Galigniana, M.D. Morishima, Y. Gallay, P.A. Pratt, W.B.
author_facet	Galigniana, M.D. Morishima, Y. Gallay, P.A. Pratt, W.B.
author_sort	Galigniana, M.D.
title	Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
title_short	Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
title_full	Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
title_fullStr	Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
title_full_unstemmed	Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
title_sort	cyclophilin-a is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
publishDate	2004
url	http://hdl.handle.net/20.500.12110/paper_00219258_v279_n53_p55754_Galigniana
work_keys_str_mv	AT galignianamd cyclophilinaisboundthroughitspeptidylprolylisomerasedomaintothecytoplasmicdyneinmotorproteincomplex AT morishimay cyclophilinaisboundthroughitspeptidylprolylisomerasedomaintothecytoplasmicdyneinmotorproteincomplex AT gallaypa cyclophilinaisboundthroughitspeptidylprolylisomerasedomaintothecytoplasmicdyneinmotorproteincomplex AT prattwb cyclophilinaisboundthroughitspeptidylprolylisomerasedomaintothecytoplasmicdyneinmotorproteincomplex
_version_	1769810160592617472

Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex

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