IBYME   02675
INSTITUTO DE BIOLOGIA Y MEDICINA EXPERIMENTAL
Unidad Ejecutora - UE
artículos
Título:
Molecular chaperone activity of TPR-domain immunophilins
Autor/es:
ERLEJMAN AG; LAGADARI M; COX, M.B.; GALIGNIANA M.
Revista:
CURRENT PROTEIN AND PEPTIDE SCIENCE
Editorial:
BENTHAM SCIENCE PUBL LTD
Referencias:
Lugar: Oak Park; Año: 2012
ISSN:
1389-2037
Resumen:
FKBP51 and FKBP52 are TPR-domain proteins belonging to a diverse family of regulators of
steroid hormone receptor signaling, including receptor maturation, hormone binding and nuclear
translocation. TPR-domain proteins are characterized for the presence of 34 amino acid repeats,
those showing a peptidyl-prolyl isomerase domain being named TPR-immunophilins. Although
structurally similar, they are functionally divergent, which is largely attributed to differences in
the FK1 domain and the proline-rich loop. FKBP51 and FKBP52 are archetype factors of this
family. They have emerged as likely contributors to a variety of hormone-dependent diseases,
including stress-related diseases, immune function, reproductive functions and a variety of
cancers. In addition, recent studies have implicated FKBP51 and FKBP52 in Alzheimers disease
and other protein aggregation disorders. Both proteins are able to interact with 90-kDa heatshock
protein Hsp90, and many of the biological actions of both immunophilins are close-related
to such functional association. This article analyzes our current understanding of FKBP51 and
FKBP52 interactions within the receptorhaperone complex, their contributions to health and
disease, and their potential as therapeutic targets for the treatment of these diseases.