ArticleProceedings of the National Academy of Sciences of the United States of America1995
A single phosphotyrosine residue of the prolactin receptor is responsible for activation of gene transcription.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 114 citations in OpenAlex.
- Identification of prolactin receptor variants with diverse effects on receptor signalling.Journal of molecular endocrinology · 2023Article
- Prolactin receptor gene transcriptional control, regulatory modalities relevant to breast cancer resistance and invasiveness.Frontiers in endocrinology · 2022Review
- Prolactin and its receptor as therapeutic targets in glioblastoma multiforme.Scientific reports · 2019Article
- A Residue Quartet in the Extracellular Domain of the Prolactin Receptor Selectively Controls Mitogen-activated Protein Kinase Signaling.The Journal of biological chemistry · 2015Article
- Molecular mechanisms of prolactin and its receptor.Endocrine reviews · 2012Review
- The Dual Role of TGFβ in Human Cancer: From Tumor Suppression to Cancer Metastasis.ISRN molecular biology · 2012Review
- Prolactin signaling through the short isoform of the mouse prolactin receptor regulates DNA binding of specific transcription factors, often with opposite effects in different reproductive issues.Reproductive biology and endocrinology : RB&E · 2009Article
- Tyrosine phosphorylation of Grb2: role in prolactin/epidermal growth factor cross talk in mammary epithelial cell growth and differentiation.Molecular and cellular biology · 2009Article
- Identification of a gain-of-function mutation of the prolactin receptor in women with benign breast tumors.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- The alveolar switch: coordinating the proliferative cues and cell fate decisions that drive the formation of lobuloalveoli from ductal epithelium.Breast cancer research : BCR · 2006Review
- Stoichiometric structure-function analysis of the prolactin receptor signaling domain by receptor chimeras.Molecular and cellular biology · 1998Article
- Regulation of the rat liver sodium-dependent bile acid cotransporter gene by prolactin. Mediation of transcriptional activation by Stat5.The Journal of clinical investigation · 1997Article
- The prolactin/growth hormone receptor family: structure/function relationships.Journal of mammary gland biology and neoplasia · 1997Review
- Prolactin mediated intracellular signaling in mammary epithelial cells.Journal of mammary gland biology and neoplasia · 1997Review
- A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9.Molecular and cellular biology · 1996Article
- Modulation of growth factor receptor function by isoform heterodimerization.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- PTP1D is a positive regulator of the prolactin signal leading to beta-casein promoter activation.The EMBO journal · 1996Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the cytokine/growth hormone/prolactin (PRL) receptor superfamily are associated with cytoplasmic tyrosine kinases of the Jak family. For the PRL receptor (PRLR), after PRL stimulation, both the kinase Jak2 and the receptor undergo tyrosine phosphorylation. To assess the role of tyrosine phosphorylation of the PRLR in signal transduction, several mutant forms of the PRLR in which various tyrosine residues were changed to phenylalanine were constructed and their functional properties were investigated. We identified a single tyrosine residue located at the C terminus of the PRLR to be necessary for in vivo activation of PRL-responsive gene transcription. This clearly indicates that a phosphotyrosine residue in the cytoplasmic domain of a member of the cytokine/growth hormone/PRL receptor superfamily is directly involved in signal transduction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.