Growth hormone (GH) induces the formation of protein complexes involving Stat5, Erk2, Shc and serine phosphorylated proteins

@article{DinersteinCali2000GrowthH,
  title={Growth hormone (GH) induces the formation of protein complexes involving Stat5, Erk2, Shc and serine phosphorylated proteins},
  author={H{\'e}l{\`e}ne Dinerstein-Cali and Fatima Ferrag and Christine Kayser and Paul A. T. Kelly and Marie Catherine Postel-Vinay},
  journal={Molecular and Cellular Endocrinology},
  year={2000},
  volume={166},
  pages={89-99}
}

Serine phosphorylation of GH-activated signal transducer and activator of transcription 5a (STAT5a) and STAT5b: impact on STAT5 transcriptional activity.

The effects of STAT5b and STAT5a serine phosphorylation on STAT-stimulated gene transcription can be modulated by promoter context and, in the case ofSTAT5a, phosphorylated of serine 779, but not serine725, may serve to regulate target gene transcriptional activity.

Prostaglandin-E2 enhances EPO-mediated STAT5 transcriptional activity by serine phosphorylation of CREB.

PGE2 enhancement of EPO-induced STAT5 transactivation is mediated by the cAMP/PKA/CREB pathway and the STAT5 target genes Bcl-X, SOCS2, and SOCS3 were up-regulated by costimulation with PGE2.

Controlled synchronization of prolactin/STAT5 and AKT1/mTOR in bovine mammary epithelial cells

Evidence of prolactin/STAT5 and AKT1/mTOR synchronization is provided, establishing a direct correlation between transcription regulation and translation regulation of milk protein in bovine mammary epithelial cells.

STAT5B-mediated Growth Hormone Signaling Is Organized by Highly Dynamic Microtubules in Hepatic Cells*

The findings indicate that the labile microtubule subpopulation specifically and dynamically organizes STAT5B-mediated growth hormone signaling in hepatic cells.

Growth Hormone Induced Activation and Regulation of JAK2 and STAT Proteins

Growth hormone is an important regulator of body growth and metabolism and leads to the induction of multiple signal transduction cascades, including STAT pathways and the MAP Kinase pathway.

Growth Hormone Signal Transduction

Cross-talk among these signaling cascades in regulating specific genes suggests that GH signaling to the nucleus involves a GH-regulated signaling network.

Differential induction of transcription factors and expression of milk protein genes by prolactin and growth hormone in the mammary gland of rabbits.

The study for the first time provided the evidence that in the mammary gland both PRL and GH can induce DNA-binding activity of transcription factors other than Stats, suggesting that the amount of MAF factor in the Mammary gland can be limiting for expression of these genes.

Cross-talk among gp130 Cytokines in Adipocytes*

The results demonstrate that an inhibitory cross-talk among specific gp130 cytokines in 3T3-L1 adipocytes occurs as a result of specific degradation of LIFR via a lysosome-mediated pathway.

Effect of growth hormone on insulin signaling

References

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Growth hormone-induced tyrosyl phosphorylation and deoxyribonucleic acid binding activity of Stat5A and Stat5B.

It is demonstrated that GH induces binding of Stat5A and Stat5B, as well as Stat1, to the GAS-like element in the beta-casein promoter, and it is suggested that JAK2 kinase is required for GH-dependent tyrosyl phosphorylation of Stat 5B and, most likely, Stat 5A.

Differential activation of Stat3 and Stat5 by distinct regions of the growth hormone receptor.

The results show that a cytokine receptor can mediate differently the activation of distinct Stat proteins that could be involved in cytokine-specific effects.

Growth Hormone-promoted Tyrosyl Phosphorylation of SHC Proteins and SHC Association with Grb2 (*)

It is suggested that GH stimulates the association of SHC proteins with JAK2•GHR complexes via the SHC-SH2 domain, tyrosyl phosphorylation ofSHC proteins, and subsequent Grb2 association with SHC protein.

Extracellular signal-regulated kinase (ERK) interacts with signal transducer and activator of transcription (STAT) 5a.

It is established that serine phosphorylation of STAT5a transactivation domain, via the MAPK pathway, is a means of modifying GH-induced transcriptional activation and also clearly identify serine 780 as a target for ERK.

Requirement of serine phosphorylation for formation of STAT-promoter complexes.

Serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3, a member of the interleukin-6 family of cytokines, which binds to and activate receptors that contain a common subunit, gp130.

Grb10 Identified as a Potential Regulator of Growth Hormone (GH) Signaling by Cloning of GH Receptor Target Proteins*

The results suggest that Grb10 is a new target for a member of the cytokine receptor family that down-regulates some GH signaling pathways downstream of Jak2 and independently of Stat5.

Two Discrete Regions of Interleukin-2 (IL2) Receptor β Independently Mediate IL2 Activation of a PD98059/Rapamycin/Wortmannin-insensitive Stat5a/b Serine Kinase*

It is reported that IL2 stimulated marked phosphorylation of serine and tyrosine residues of both Stat5a and Stat5b in human T lymphocytes and in several IL2-responsive lymphocytic cell lines, suggesting that a yet-to-be-identified serine kinase mediates Stat5 a/b activation.

Mapping of Stat3 serine phosphorylation to a single residue (727) and evidence that serine phosphorylation has no influence on DNA binding of Stat1 and Stat3.

Findings do not agree with earlier claims of excess serine to tyrosine phosphorylation in activated Stats 1 and 3 or to claims of more stable DNA binding of serineosphorylated Stat dimers.

Interleukin‐2 activation of STAT5 requires the convergent action of tyrosine kinases and a serine/threonine kinase pathway distinct from the Raf1/ERK2 MAP kinase pathway.

The present data indicate that the transcriptional activity of STAT5 is regulated by serine kinases in T lymphocytes, and requires the convergent action of tyrosineKinases and a distinct serine/threonine kinase which has not previously been implicated in IL‐2 signalling.