Show simple item record Galigniana, Mario Daniel Morishima, Yoshihiro Gallay, Philippe A. Pratt, William B. 2018-02-08T13:46:16Z 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.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.subject CELL LINE
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 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/
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/pmid/15496417
dc.conicet.fuente individual

Archivos asociados

This item appears in the following Collection(s)

  • Articulos(IBYME) [1050]

Show simple item record

info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)