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Related Concept Videos

The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
Statgraphics01:10

Statgraphics

Statgraphics is a comprehensive statistical software suite designed for both basic and advanced data analysis. Originating in 1980 at Princeton University under Dr. Neil W. Polhemus, it was one of the pioneering tools for statistical computing on personal computers, with its public release in 1982 marking an early milestone in data science software. Over the years, it has evolved into a robust platform for data science, offering tools for regression analysis, ANOVA, multivariate statistics,...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: May 23, 2026

Time-resolved F&#246;rster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells
07:12

Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells

Published on: September 9, 2021

The JAK-STAT pathway at twenty.

George R Stark1, James E Darnell

  • 1Department of Molecular Genetics, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA. starkg@ccf.org

Immunity
|April 24, 2012
PubMed
Summary
This summary is machine-generated.

The Janus kinase-Signal transducer and activator of transcription (JAK-STAT) pathway, involving TYK2, JAK1, STAT1, STAT2, and IRF9, is crucial for cellular responses to interferons and cytokines. Recent research highlights STAT protein posttranslational modifications and noncanonical functions beyond transcription.

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Last Updated: May 23, 2026

Time-resolved F&#246;rster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells
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Published on: September 9, 2021

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Published on: October 4, 2018

Area of Science:

  • Immunology
  • Molecular Biology
  • Cellular Signaling

Background:

  • The JAK-STAT pathway is a critical signaling cascade initiated by interferons and cytokines.
  • Key components include tyrosine kinases (TYK2, JAK1) and transcription factors (STAT1, STAT2, IRF9).
  • This pathway exemplifies cell surface-to-nucleus information transfer for gene regulation.

Purpose of the Study:

  • To review the foundational discoveries of the JAK-STAT pathway.
  • To highlight recent advancements in understanding STAT protein regulation and function.
  • To discuss the broader roles of STAT proteins in cellular processes.

Main Methods:

  • Literature review of seminal and recent research on the JAK-STAT pathway.
  • Analysis of studies on interferon and cytokine signaling mechanisms.
  • Examination of research on STAT protein posttranslational modifications and noncanonical functions.

Main Results:

  • Established the role of TYK2, JAK1, STAT1, STAT2, and IRF9 in type I interferon response.
  • Demonstrated conserved signaling mechanisms across different interferons and cytokines via the JAK-STAT pathway.
  • Revealed diverse posttranslational modifications of STAT proteins (phosphorylation, acetylation, methylation, sumoylation).
  • Identified noncanonical functions of STAT proteins in transcriptional regulation, mitochondrial respiration, and chromatin organization.

Conclusions:

  • The JAK-STAT pathway is a fundamental paradigm for cytokine signal transduction.
  • STAT proteins are highly versatile, with complex regulatory networks involving posttranslational modifications.
  • STAT proteins possess significant non-transcriptional roles impacting cellular respiration and chromatin structure.