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Related Concept Videos

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.
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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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...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
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Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Mutually exclusive STAT1 modifications identified by Ubc9/substrate dimerization-dependent SUMOylation.

Susan Zimnik1, Matthias Gaestel, Rainer Niedenthal

  • 1Institute for Physiological Chemistry/Biochemistry, Medical School Hannover, Carl-Neuberg Strasse 1, 30625 Hannover, Germany.

Nucleic Acids Research
|January 29, 2009
PubMed
Summary
This summary is machine-generated.

Phosphorylation of STAT1 at Y701 and SUMOylation at K703 are mutually exclusive events. This finding reveals how STAT1 activity is regulated through distinct post-translational modifications in vivo.

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Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Post-Translational Modifications

Background:

  • Signal transducer and activator of transcription (STAT) proteins are crucial in cellular signaling.
  • STAT1 activity is regulated by post-translational modifications like phosphorylation and SUMOylation.
  • Previous work showed SUMOylation at K703 inhibits Y701 phosphorylation, but the reverse effect was unknown.

Purpose of the Study:

  • To investigate the influence of STAT1 Y701 phosphorylation on K703 SUMOylation in vivo.
  • To develop a novel system for studying SUMOylation in vivo.

Main Methods:

  • Development of a Ubc9/substrate dimerization-dependent SUMOylation (USDDS) system.
  • Co-expression of FKBP-fusion proteins (including STAT1) and Ubc9-FRB in HEK293 cells.
  • Induction of SUMOylation using AP21967 and analysis of STAT1 phosphorylation via interferon-beta treatment.

Main Results:

  • The USDDS system successfully induced in vivo SUMOylation of various proteins, including STAT1 and p53, at their specific sites.
  • STAT1 phosphorylation at Y701, induced by interferon-beta, significantly inhibited SUMOylation at K703.
  • Y701 phosphorylation and K703 SUMOylation were shown to be mutually exclusive modifications on STAT1.

Conclusions:

  • STAT1 phosphorylation at Y701 and SUMOylation at K703 are mutually exclusive modifications.
  • These opposing modifications prevent signal integration and ensure regulated STAT1 nuclear-cytoplasmic shuttling.
  • This mechanism contributes to the generation of functionally distinct STAT1 subpopulations.