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dc.contributor.author
Galigniana, Mario Daniel
dc.contributor.author
Morishima, Yoshihiro
dc.contributor.author
Gallay, Philippe A.
dc.contributor.author
Pratt, William B.
dc.date.available
2018-02-08T13:46:16Z
dc.date.issued
2004-10-20
dc.identifier.citation
Galigniana, Mario Daniel; Morishima, Yoshihiro; Gallay, Philippe A.; Pratt, William B.; Cyclophilin-A is bound to through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 53; 20-10-2004; 55754-55759
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/36095
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Cell Line
dc.subject
Immunosuppressive Agents
dc.subject
Microtubules
dc.subject
Tumor Suppessor Protein P53
dc.subject
Clyclophilin
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Cyclophilin-A is bound to through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-12-28T13:40:09Z
dc.identifier.eissn
1083-351X
dc.journal.volume
279
dc.journal.number
53
dc.journal.pagination
55754-55759
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Baltimore
dc.description.fil
Fil: Galigniana, Mario Daniel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of Michigan; Estados Unidos
dc.description.fil
Fil: Morishima, Yoshihiro. University of Michigan; Estados Unidos
dc.description.fil
Fil: Gallay, Philippe A.. The Scripps Research Institute; Estados Unidos
dc.description.fil
Fil: Pratt, William B.. University of Michigan; Estados Unidos
dc.journal.title
Journal of Biological Chemistry (online)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/279/53/55754.long
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M406259200
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/pmid/15496417


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