Progesterone Receptor Contains a Proline-Rich Motif that Directly Interacts with SH3 Domains and Activates c-Src Family Tyrosine Kinases
Steroid hormones have rapid nongenomic effects on cell-signaling pathways, but the receptor mechanisms responsible for this are not understood. We have identified a specific polyproline motif in the amino-terminal domain of conventional progesterone receptor (PR) that mediates direct progestin-depen...
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| Veröffentlicht in: | Molecular cell 2001-08, Vol.8 (2), p.269-280 |
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| creator | Boonyaratanakornkit, Viroj Scott, Margaret Porter Ribon, Vered Sherman, Lori Anderson, Steven M Maller, James L Miller, W.Todd Edwards, Dean P |
| description | Steroid hormones have rapid nongenomic effects on cell-signaling pathways, but the receptor mechanisms responsible for this are not understood. We have identified a specific polyproline motif in the amino-terminal domain of conventional progesterone receptor (PR) that mediates direct progestin-dependent interaction of PR with SH3 domains of various cytoplasmic signaling molecules, including c-Src tyrosine kinases. Through this interaction, PR is a potent activator of Src kinases working by an SH3 domain displacement mechanism. By mutagenesis, we also show that rapid progestin-induced activation of Src and downstream MAP kinase in mammalian cells is dependent on PR-SH3 domain interaction, but not on the transcriptional activity of PR. Preliminary evidence for the biological significance of this PR signaling pathway through regulatory SH3 domains was shown with respect to an influence on progestin-induced growth arrest of breast epithelial cells and induction of
Xenopus oocyte maturation. |
| doi_str_mv | 10.1016/S1097-2765(01)00304-5 |
| format | Article |
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Xenopus oocyte maturation.</description><subject>Amino Acid Motifs</subject><subject>Animals</subject><subject>Breast Neoplasms</subject><subject>Cell Line</subject><subject>Female</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Models, Biological</subject><subject>Mutagenesis, Site-Directed</subject><subject>Oocytes - drug effects</subject><subject>Oocytes - physiology</subject><subject>Progesterone - pharmacology</subject><subject>Progesterone Congeners - pharmacology</subject><subject>Promegestone - pharmacology</subject><subject>Protein-Tyrosine Kinases - genetics</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins - genetics</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-hck</subject><subject>Receptors, Progesterone - chemistry</subject><subject>Receptors, Progesterone - genetics</subject><subject>Receptors, Progesterone - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Signal Transduction</subject><subject>src Homology Domains - physiology</subject><subject>src-Family Kinases</subject><subject>Transfection</subject><subject>Two-Hybrid System Techniques</subject><subject>Xenopus</subject><subject>Xenopus laevis - physiology</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9uEzEQxleIipbCI4B8QnDYdia219kTqlJKK1qBmtwtr3dCjHbt1HaK8gY8Ns4fiSOnsUa_b8bzfVX1DuECAZvLOUKr6olq5EfATwAcRC1fVGf7tsBGvDy-d8hp9TqlXwAo5LR9VZ0iSiEVh7Pqz48YflLKFIMn9kiW1jlENgs-G-cTM6wAg_NUPzq7Yg8huyXLK5PZtYtk87Bld76ojc2J_XZ5xea3nF2H8aD2Pbuy2T2bTInZeh4tuzGjK6rFNoZU5rJvzptE6U11sjRDorfHel4tbr4sZrf1_fevd7Or-9qKFnNtYIoWsDeTThJvOsU7rnopOElJrcKukaptLHKzVKK3opGTzoIC2arWWMHPqw-HsesYnjblcD26ZGkYjKewSRqnCHzCoYDyANryzxRpqdfRjSZuNYLeJaD3CeidvRpQ7xPQsujeHxdsupH6f6qj5QX4fACoXPnsKOpkHXlL_d5Q3Qf3nxV_AahDlkg</recordid><startdate>20010801</startdate><enddate>20010801</enddate><creator>Boonyaratanakornkit, Viroj</creator><creator>Scott, Margaret Porter</creator><creator>Ribon, Vered</creator><creator>Sherman, Lori</creator><creator>Anderson, Steven M</creator><creator>Maller, James L</creator><creator>Miller, W.Todd</creator><creator>Edwards, Dean P</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope></search><sort><creationdate>20010801</creationdate><title>Progesterone Receptor Contains a Proline-Rich Motif that Directly Interacts with SH3 Domains and Activates c-Src Family Tyrosine Kinases</title><author>Boonyaratanakornkit, Viroj ; 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We have identified a specific polyproline motif in the amino-terminal domain of conventional progesterone receptor (PR) that mediates direct progestin-dependent interaction of PR with SH3 domains of various cytoplasmic signaling molecules, including c-Src tyrosine kinases. Through this interaction, PR is a potent activator of Src kinases working by an SH3 domain displacement mechanism. By mutagenesis, we also show that rapid progestin-induced activation of Src and downstream MAP kinase in mammalian cells is dependent on PR-SH3 domain interaction, but not on the transcriptional activity of PR. Preliminary evidence for the biological significance of this PR signaling pathway through regulatory SH3 domains was shown with respect to an influence on progestin-induced growth arrest of breast epithelial cells and induction of
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Motifs Animals Breast Neoplasms Cell Line Female Humans Immunoblotting Mitogen-Activated Protein Kinases - metabolism Models, Biological Mutagenesis, Site-Directed Oocytes - drug effects Oocytes - physiology Progesterone - pharmacology Progesterone Congeners - pharmacology Promegestone - pharmacology Protein-Tyrosine Kinases - genetics Protein-Tyrosine Kinases - metabolism Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-hck Receptors, Progesterone - chemistry Receptors, Progesterone - genetics Receptors, Progesterone - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Signal Transduction src Homology Domains - physiology src-Family Kinases Transfection Two-Hybrid System Techniques Xenopus Xenopus laevis - physiology |
| title | Progesterone Receptor Contains a Proline-Rich Motif that Directly Interacts with SH3 Domains and Activates c-Src Family Tyrosine Kinases |
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