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Your search keyword '"Savouret, J.-F."' showing total 3 results
Start Over Author "Savouret, J.-F." Topic nuclear proteins
3 results on '"Savouret, J.-F."'

1. Regulation of the progesterone receptor functions.

Author

Savouret JF, Muchardt C, Quesne M, Mantel A, De The H, and Milgrom E

Subjects
Animals, Humans, Neoplasm Proteins physiology, Promyelocytic Leukemia Protein, Receptors, Progesterone genetics, Transcription Factors physiology, Transcriptional Activation, Tumor Suppressor Proteins, Nuclear Proteins, Promoter Regions, Genetic, Receptors, Progesterone physiology
Published
1998
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2. [Effect of PML and PML-RAR on the transactivation properties and subcellular localization of steroid hormone receptors].

Author

Guiochon-Mantel A, Savouret JF, Quignon F, Delabre K, Milgrom E, and De The H

Subjects
In Vitro Techniques, Receptors, Progesterone analysis, Receptors, Progesterone genetics, Receptors, Progesterone metabolism, Subcellular Fractions metabolism, Tissue Distribution, Transcription Factors genetics, Transcription, Genetic drug effects, Transcriptional Activation, Tumor Suppressor Proteins, Leukemia, Promyelocytic, Acute genetics, Neoplasm Proteins pharmacology, Nuclear Proteins, Oncogene Proteins, Fusion pharmacology, Receptors, Steroid genetics, Transcription Factors pharmacology
Abstract

PML is a protein involved in the t (15, 17) translocation of promyelocytic leukemia and is mainly localized in nuclear bodies. Here we show that PML exerts a very powerful enhancing activity (up to 20-fold) on the transactivating properties of the progesterone receptor (PR) and has a similar effect on several other steroid hormone receptors. There is probably a direct or indirect interaction between PR and PML since when the latter was expressed at high concentrations it shifted PR into the nuclear bodies. Use of deletion mutants showed that both activation functions (AF1 and AF2) of PR as well as the coiled coil and His-Cys rich domains of PML were required for transcriptional enhancement. The fusion protein PML-RAR, which is not localized in nuclear bodies, also enhanced the transactivating activity of PR but this effect was totally suppressed by the administration of retinoic acid. PML, which is ubiquitously expressed, may thus be involved in the transactivation properties of steroid hormone receptors. This mechanism may also play a role in the oncogenic properties of PML-RAR and in their suppression by the retinoic acid.

Published
1996

3. Effect of PML and PML-RAR on the transactivation properties and subcellular distribution of steroid hormone receptors.

Author

Guiochon-Mantel A, Savouret JF, Quignon F, Delabre K, Milgrom E, and De The H

Subjects
Animals, Base Sequence, CHO Cells, Cell Line, Cricetinae, HeLa Cells, Humans, Molecular Sequence Data, Promyelocytic Leukemia Protein, Receptors, Progesterone genetics, Receptors, Progesterone physiology, Receptors, Retinoic Acid genetics, Recombinant Fusion Proteins, Transcription Factors genetics, Transcription Factors metabolism, Transcription, Genetic drug effects, Transcriptional Activation, Transfection, Tumor Suppressor Proteins, Neoplasm Proteins, Nuclear Proteins, Receptors, Retinoic Acid physiology, Transcription Factors pharmacology
Abstract

PML (promyelocytic leukemia) is a protein involved in the t (15;17) translocation of promyelocytic leukemia and is mainly localized in nuclear bodies. Here we show that PML exerts a very powerful enhancing activity (up to 20-fold) on the transactivating properties of the progesterone receptor (PR) and has a similar effect on several other steroid hormone receptors. There is probably a direct or indirect interaction between PR and PML, because when the latter was expressed at high concentrations it shifted PR into the nuclear bodies. The use of deletion mutants showed that both activation functions (AF1 and AF2) of PR as well as the coiled coil and His-Cys-rich domains of PML were required for transcriptional enhancement. The fusion protein PML-RAR which is not localized in nuclear bodies, also enhanced the transactivating activity of PR, but this effect was totally suppressed by the administration of retinoic acid. PML, which is ubiquitously expressed, may thus be involved in the transactivation properties of steroid hormone receptors. This mechanism may also play a role in the oncogenic properties of PML-RAR and in their suppression by retinoic acid.

Published
1995
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