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Only a small portion of the cytoplasmic progesterone receptor is associated with Hsp90 in vivo by Satu Passinen; Marjaana Haverinen; Anu Pekki; Jenita Rauta; Jorma Paranko; Heimo Syvälä; Pentti Tuohimaa; Timo Ylikomi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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In cell extracts all of the nonliganded steroid receptor molecules are found as an oligomeric complex with Hsp90 and other proteins. In previous studies we have shown that Wild-type Hsp90 and progesterone receptor (PR) are located in different cell compartments (Tuohimaa et al. [1993] Proc. Natl. Acad. Sci. USA 90:5848-5852). In the present work we studied whether PR and Hsp90 can efficiently associate provided they are present in the same cell compartment. The association of Hsp90 with PR in vivo was studied by nuclear cotranslocation and immunohistochemistry with an antibody (␣D) which can distinguish between the oligomeric and dissociated form. Upon expression of a cytoplasmic mutant of PR with Wild-type (cytoplasmic) Hsp90 and Wild-type (nuclear) PR with NLS-Hsp90 (a Hsp90 with a nuclear localization signal), we noted that the epitope of ␣D in PR was exposed in both cases. Also, in vivo crosslinking and treatment of cells with substances which stabilize the oligomeric complex in vitro were inefficient in demonstrating or inducing a similar oligomeric receptor form detectable in vitro in cell homogenates. However, when the cytoplasmic PR mutant (⌬PR) was coexpressed with a nucle

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Author

Satu Passinen; Marjaana Haverinen; Anu Pekki; Jenita Rauta; Jorma Paranko; Heimo Syvälä; Pentti Tuohimaa; Timo Ylikomi

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)