The last proline of Box 1 is essential for association with JAK2 and functional activation of the prolactin receptor

Pezet, Alain; Buteau, Hélène; Kelly, Paul A.; Edery, Marc

doi:10.1016/s0303-7207(97)00063-4

Cited by 68 publications

(39 citation statements)

References 43 publications

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“…The ICD of sbPRLR comprises 284 amino acids and contains the proline-rich motif (box 1), which shares 100% identity with all PRLRs known so far. This is by far the most highly conserved region within the PRLRs ICD among cytokine receptors and it plays an important role in the signal transduction pathway (Dinerstein et al, 1995;Pezet et al, 1997). The ICD of different PRLR forms varies in size and several isoforms of PRLR which differ from each other in length and composition have been found in the same species (Boutin et al, , 1988Shirota et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Santos

Ingleton²,

Cavaco

et al. 2001

General and Comparative Endocrinology

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The prolactin receptor (PRLR) was cloned and its tissue distribution characterized in adults of the protandrous hermaphrodite marine teleost, the sea bream (Sparus aurata). An homologous cDNA probe for sea bream PRLR (sbPRLR) was obtained by RT-PCR using gill mRNA. This probe was used to screen intestine and kidney cDNA libraries from which two overlapping clones (1100 and 2425 bp, respectively) were obtained. These clones had 100% sequence identity in the overlapping region (893 bp) and were used to deduce the complete amino acid sequence of sbPRLR. The receptor spans 2640 bp and encodes a protein of 537 amino acids. Features characteristic of PRLR, two pairs of cysteines, WS box, hydrophobic transmembrane domain, box 1, and box 2, were identified and showed a high degree of sequence identity to PRLRs from other vertebrate species. SbPRLR is 29 and 32% identical to tilapia (Oreochromis niloticus) and goldfish (Carassius auratus) PRLRs, respectively. In the sea bream two PRLR transcripts of 2.8 and 3.2 kb were detected in the intestine, kidney, and gills and a single transcript of 2.8 kb was detected in skin and pituitary by Northern blot. Spermiating gonads (more than 95% male tissue; gonado-somatic index of 0.6) contained, in addition to the 2.8-kb transcript, three more transcripts of 1.9, 1.3, and 1.1 kb. RT-PCR, which is a far more sensitive method than Northern blot, detected PRLR mRNA in gills, intestine, brain, pituitary, kidney, liver, gonads, spleen, head-kidney, heart, muscle, and bone. Immunohistochemistry using specific polyclonal antibodies raised against an oligopeptide from the extracellular domain of sbPRLR detected PRLR in several epithelial tissues of juvenile sea bream, including the anterior gut, renal tubule, choroid membrane of the third ventricle, saccus vasculosus, branchial chloride cells, and branchial cartilage.

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Section: Discussionmentioning

confidence: 99%

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Santos

Ingleton²,

Cavaco

et al. 2001

General and Comparative Endocrinology

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“…6A). For a detailed analysis of the kinase recruitment domain, we substituted conserved amino acids within the box motif (22)(23)(24) of the short IL-31R␣ isoform by alanines and tested the responsiveness to IL-31 in STAT3 reporter gene assays. The mutation W586A resulted in a diminished signal.…”

Section: Identification Of Critical Residues Within the Box Motif Of mentioning

confidence: 99%

Prerequisites for Functional Interleukin 31 Signaling and Its Feedback Regulation by Suppressor of Cytokine Signaling 3 (SOCS3)

Maier

Mittermeir

Ess

et al. 2015

Journal of Biological Chemistry

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Background: Signaling by IL-31 involves OSMR␤ and IL-31R␣, which is expressed in different isoforms. Results: Four of five membrane-bound isoforms activate IL-31 signaling, which is counter-regulated by SOCS3. Conclusion: IL-31 responsiveness is controlled by the expression of specific IL-31R␣ isoforms and is negatively regulated by SOCS proteins. Significance: This study provides new insights into the regulation of IL-31 signaling.

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“…[27][28][29][30]. The recently cloned short forms of the receptor contain a box 1 domain (23,24), which in the long form is required for the activation of JAK2 (30,31). Theoretically therefore, each short form has the potential to activate extracellular signal-regulated kinase 1 and 2 (ERK1/2) via the Ras/ Raf pathway.…”

Section: Introductionmentioning

confidence: 99%

S179D Prolactin Increases Vitamin D Receptor and p21 through Up-regulation of Short 1b Prolactin Receptor in Human Prostate Cancer Cells

Ginsburg

Vonderhaar

et al. 2005

Cancer Research

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In this study, we further investigated the mechanisms by which pseudophosphorylated prolactin (S179D PRL) inhibits the growth of human prostate cancer cells. When treated with S179D PRL for 3 days, LnCAP cells responded by increasing expression of the vitamin D receptor (VDR) and the cell cycle regulatory molecule, p21, whereas PC3 and DU145 cells did not. After 5 days of treatment, both PC3 and DU145 cells responded. Untreated LnCAP cells express the short 1b form (SF1b) of the human prolactin receptor, but DU145 and PC3 cells express only low amounts of this receptor until elevated by treatment with S179D PRL. DU145 and PC3 cells become sensitive to the negative effects of S179D PRL on cell number after induction of the SF1b. Transfection of either SF1b or SF1a into PC3 or DU145 cells made them sensitive to S179D PRL in the 3-day time frame, a finding that was not duplicated by transfection with the long form of the receptor. Treatment of LnCAP cells with S179D PRL increased long-term activation of extracellular signal-regulated kinase 1/2 (ERK1/2). This did not occur in PC3 and DU145 cells until transfection with SF1a/ SF1b. Blockade of ERK signaling eliminated S179D PRLstimulated expression of the VDR and p21 in LnCAP cells and transfected PC3 and DU145 cells. We conclude that initiation of alternative splicing to produce SF1b, and subsequent altered signaling, contribute to the growth inhibitory mechanisms of S179D PRL. This is the first indication of a role for short prolactin receptors in the regulation of cell proliferation. (Cancer Res 2005; 65(16): 7509-15)

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The last proline of Box 1 is essential for association with JAK2 and functional activation of the prolactin receptor

Cited by 68 publications

References 43 publications

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Cloning, Characterization, and Tissue Distribution of Prolactin Receptor in the Sea Bream (Sparus aurata)

Prerequisites for Functional Interleukin 31 Signaling and Its Feedback Regulation by Suppressor of Cytokine Signaling 3 (SOCS3)

S179D Prolactin Increases Vitamin D Receptor and p21 through Up-regulation of Short 1b Prolactin Receptor in Human Prostate Cancer Cells

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