Related Experiment Video

Updated: Mar 6, 2026

Merging Absolute and Relative Quantitative PCR Data to Quantify STAT3 Splice Variant Transcripts
11:19

Merging Absolute and Relative Quantitative PCR Data to Quantify STAT3 Splice Variant Transcripts

Published on: October 9, 2016

15.6K

STAT5-Interacting Proteins: A Synopsis of Proteins that Regulate STAT5 Activity

Ashley A Able1,2, Jasmine A Burrell3,4, Jacqueline M Stephens5,6

  • 1Adipocyte Biology Laboratory, Pennington Biomedical Research Center, Baton Rouge, LA 70808, USA. Ashley.Able@pbrc.edu.

Biology
|March 14, 2017
PubMed

Insights

Signal Transducers and Activators of Transcription (STATs), particularly STAT5A and STAT5B, regulate vital cellular processes. This review explores how interacting proteins modulate STAT5 activity through physical interactions and phosphorylation.

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Gene Regulation

Background:

  • Signal Transducers and Activators of Transcription (STATs) are crucial mediators in the JAK/STAT pathway.
  • STAT5A and STAT5B play significant roles in cellular differentiation, adipogenesis, oncogenesis, and immune responses.
  • STAT5 activity is influenced by interactions with a diverse range of proteins.

Purpose of the Study:

  • To review the mechanisms by which proteins physically interacting with STAT5 modulate its activity.
  • To elucidate the roles of coactivators, corepressors, and regulatory proteins in STAT5 signaling.
  • To highlight the impact of phosphorylation and dephosphorylation by interacting proteins on STAT5 function.

Main Methods:

  • Literature review of studies investigating STAT5 protein interactions.
  • Analysis of research on STAT5 phosphorylation and dephosphorylation events.
  • Synthesis of findings on how protein interactions affect STAT5 transcriptional activity.

Main Results:

  • STAT5 interactions with receptors, regulators, kinases, and phosphatases are key to its function.
  • Interacting proteins act as coactivators or corepressors, fine-tuning STAT5 transcriptional output.
  • Specific proteins positively or negatively regulate STAT5 signaling via phosphorylation or dephosphorylation.

Conclusions:

  • Protein-protein interactions are central to the regulation of STAT5 activity.
  • Understanding these interactions provides insights into STAT5's role in various physiological and pathological processes.
  • Modulation of STAT5 activity by interacting proteins offers potential therapeutic targets.
Keywords:
JAKSTATssignaling

More Related Videos

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis10:22

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

Published on: August 15, 2013

31.4K
Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization08:57

Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization

Published on: October 6, 2019

10.8K

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...
13.5K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

2.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.8K
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
8.8K
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

3.2K