A limited cytoplasmic region of the prolactin receptor critical for signal transduction
| Autor: | Paul A. Kelly, Jacqueline Paly, Corinne Levi-Meyrueis, Marc Edery, Jean Djiane |
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| Přispěvatelé: | Unité de biologie cellulaire et moléculaire, Institut National de la Recherche Agronomique (INRA) |
| Rok vydání: | 1994 |
| Předmět: |
endocrine system
DNA Complementary Receptors Prolactin [SDV]Life Sciences [q-bio] Molecular Sequence Data Mutant CHO Cells Biology Biochemistry Radioligand Assay 03 medical and health sciences Endocrinology Cricetinae Escherichia coli Consensus sequence Animals Humans Point Mutation Coding region Amino Acid Sequence Receptor Molecular Biology ComputingMilieux_MISCELLANEOUS Cells Cultured 030304 developmental biology 0303 health sciences Prolactin receptor 030302 biochemistry & molecular biology Molecular biology Prolactin Transmembrane domain Signal transduction Cytokine receptor hormones hormone substitutes and hormone antagonists Signal Transduction |
| Zdroj: | Molecular and Cellular Endocrinology Molecular and Cellular Endocrinology, Elsevier, 1994, 102, pp.39-44 |
| ISSN: | 0303-7207 |
| DOI: | 10.1016/0303-7207(94)90095-7 |
| Popis: | Prolactin receptors (PRL-R) are members of the cytokine receptor superfamily, which have in common, an absence of any known consensus sequence for signal transduction in their cytoplasmic domains. Four areas of high sequence homology have been identified in the cytoplasmic domains of PRL and growth hormone (GH) receptors, which may be important for signal transduction. The aim of this study was to investigate the role of these cytoplasmic regions in the functional activity of the PRL-R. Several mutant forms of PRL-R were constructed either by truncation or by deletion of the cDNA. Biological activities of these mutant receptors were assayed in CHO cells using a functional assay consisting in the co-transfection of PRL-R cDNA, along with a PRL responsive promoter fused to the coding sequence of the chloramphenicol acetyl transferase (CAT) gene. Progressive truncation of the cytoplasmic domain led to a progressive loss of ability to transactivate the CAT gene. Fully active PRL-R could be obtained when 217 of 358 aa of the cytoplasmic domain were present. Deletion of the first region of homology with the GH-R (residues 245–267) abolished the functional activity of PRL-R, whereas deletion of the second region of homology (residues 322–333) was without effect. These results indicate that a critical cytoplasmic region of 23 residues proximal to the transmembrane domain is essential for PRL signal transduction. There is strong homology within an 8-residue segment of this region with other members of the cytokine receptor superfamily, suggesting it contains a sequence necessary for signal transduction. |
| Databáze: | OpenAIRE |
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