ArticleMolecular endocrinology (Baltimore, Md.)2008
The extracellular domain of the growth hormone receptor interacts with coactivator activator to promote cell proliferation.
Article in Molecular endocrinology (Baltimore, Md.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 51 citations in OpenAlex.
- Growth hormone receptor antagonists, GHA2 and GHA3, with dual activity against the human and mouse receptor.Protein science : a publication of the Protein Society · 2025Article
- A Recurrent Mutation in Growth Hormone Receptor (The Yale journal of biology and medicine · 2023Article
- The growth hormone receptor interacts with transcriptional regulator HMGN1 upon GH-induced nuclear translocation.Journal of cell communication and signaling · 2023Article
- The Cellular Behavior, Intracellular Signaling Profile and Nuclear-Targeted Potential Functions of Porcine Growth Hormone (pGH) in Swine Testicular Cells.Cell biochemistry and biophysics · 2022Article
- The effect of heat stress on the cellular behavior, intracellular signaling profile of porcine growth hormone (pGH) in swine testicular cells.Cell stress & chaperones · 2022Article
- Genetic Code Expansion Enables Site-Specific PEGylation of a Human Growth Hormone Receptor Antagonist through Click Chemistry.Bioconjugate chemistry · 2020Article
- Medical Treatment with Somatostatin Analogues in Acromegaly: Position Statement.Endocrinology and metabolism (Seoul, Korea) · 2019Review
- Growth Hormone Receptor Mutations Related to Individual Dwarfism.International journal of molecular sciences · 2018Review
- Porcine growth hormone induces the nuclear localization of porcine growth hormone receptorAsian-Australasian journal of animal sciences · 2018Article
- The Growth Hormone Receptor: Mechanism of Receptor Activation, Cell Signaling, and Physiological Aspects.Frontiers in endocrinology · 2018Review
- Ultradian glucocorticoid exposure directs gene-dependent and tissue-specific mRNA expression patterns in vivo.Molecular and cellular endocrinology · 2017Article
- Let-7b Regulates Myoblast Proliferation by InhibitingFrontiers in physiology · 2017Article
- Article
- Minireview: mechanisms of growth hormone-mediated gene regulation.Molecular endocrinology (Baltimore, Md.) · 2014Review
- Hypoxia and cytoplasmic alkalinization upregulate growth hormone expression in lymphocytes.Cellular immunology · 2013Article
- HMGN2 inducibly binds a novel transactivation domain in nuclear PRLr to coordinate Stat5a-mediated transcription.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Nuclear receptor coactivators: structural and functional biochemistry.Biochemistry · 2011Review
- The growth hormone receptor: mechanism of activation and clinical implications.Nature reviews. Endocrinology · 2010Review
- Acromegaly pathogenesis and treatment.The Journal of clinical investigation · 2009Review
- O-Glycosylated 24 kDa human growth hormone has a mucin-like biantennary disialylated tetrasaccharide attached at Thr-60.Proteomics · 2009Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presence of GH receptor (GHR) in the cell nucleus correlates with cell division, and targeting the GHR to the nucleus results in constitutive proliferation and transformation because of increased sensitivity to autocrine GH. Here we have sought additional mechanisms that might account for the enhanced proliferation seen with nuclear GHR, commencing with a yeast two-hybrid (Y2H) screen for interactors with the extracellular domain of the GHR [GH-binding protein (GHBP)]. We find that the GHBP is a transcriptional activator in yeast and mammalian cells, and this activity resides in the lower cytokine receptor module. Activity is dependent on S226, the conserved serine of the cytokine receptor consensus WSXWS box. By using parallel GHBP affinity columns and tandem mass spectrometry of tryptic digests of proteins bound to wild-type GHBP and S226A columns, we identified proteins that bind to the transcriptionally active GHBP. These include a nucleoporin and two transcriptional regulators, notably the coactivator activator (CoAA), which is also an RNA binding splicing protein. Binding of CoAA to the GHBP was confirmed by glutathione S-transferase pulldown and coimmunoprecipitation, and shown to be GH dependent in pro-B Ba/F3 cells. Importantly, stable expression of CoAA in Ba/F3 cells resulted in an increased maximum proliferation in response to GH, but not IL-3. Because CoAA overexpression has been identified in many cancers and its stable expression promotes cell proliferation and cell transformation in NIH-3T3 cells, we suggest CoAA contributes to the proliferative actions of nuclear GHR by the hormone-dependent recruitment of this powerful coactivator to the GHR.
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