What question did this study set out to answer?

To elucidate the molecular mechanisms by which the immunophilins FKBP51 and FKBP52 differentially regulate glucocorticoid receptor trafficking and transcriptional activity in mammalian cells.

February 1, 2005Journal of Biological ChemistryOpen Access

FK506-binding Proteins 51 and 52 Differentially Regulate Dynein Interaction and Nuclear Translocation of the Glucocorticoid Receptor in Mammalian Cells

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Authors

GWGabriela M. WochnikMax Planck Society JRJoëlle RüeggUppsala University GAG. AbelBionorica (Germany)

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Implication

Cellular study reveals differential regulation of glucocorticoid receptor translocation and dynein binding by FKBP51 and FKBP52 in mammalian cells, suggesting opposing roles in steroid signaling.

Key Points

To elucidate the molecular mechanisms by which the immunophilins FKBP51 and FKBP52 differentially regulate glucocorticoid receptor trafficking and transcriptional activity in mammalian cells.
Assayed glucocorticoid receptor transcriptional activity and nuclear translocation kinetics in mammalian cell cultures following altered expression of FKBP51 and FKBP52.
Performed mutational analysis, domain swapping between FKBP51 and FKBP52, and coexpression of dynamitin and isolated peptidylprolyl isomerase (PPIase) domains to evaluate dynein and Hsp90 interactions.
FKBP51 overexpression reduced glucocorticoid receptor transcriptional activity and delayed nuclear translocation, correlating with reduced interaction with the motor protein dynein relative to FKBP52.
FKBP52 mitigated FKBP51-induced receptor inhibition, whereas disrupting dynein transport via dynamitin or the FKBP52 PPIase domain fragment decreased receptor activity.
Efficient receptor signaling required Hsp90 interaction, dynein association, and PPIase activity, with domain swapping between FKBP51 and FKBP52 reversing their characteristic functional effects.

Cite This Study

Wochnik et al. (2005) studied this question.

synapsesocial.com/papers/6a7fb39a69e70e12e918f296 https://doi.org/10.1074/jbc.m407498200

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Implication

Cellular study reveals differential regulation of glucocorticoid receptor translocation and dynein binding by FKBP51 and FKBP52 in mammalian cells, suggesting opposing roles in steroid signaling.

FK506-binding Proteins 51 and 52 Differentially Regulate Dynein Interaction and Nuclear Translocation of the Glucocorticoid Receptor in Mammalian Cells

Discussion

Member takes

Implication

Key Points

Cite This Study

FK506-binding Proteins 51 and 52 Differentially Regulate Dynein Interaction and Nuclear Translocation of the Glucocorticoid Receptor in Mammalian Cells

Discussion

Member takes

Implication

Key Points

Cite This Study

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