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Proteomic analysis of SETD6 interacting proteins.

Ofir Cohn1, Ayelet Chen1, Michal Feldman1

  • 1The Shraga Segal Department of Microbiology, Immunology and Genetics, Israel; The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, P.O.B. 653, Be׳er-Sheva, 84105 Israel.

Data in Brief
|March 4, 2016
PubMed
Summary

Researchers identified new proteins interacting with SETD6 (SET-domain-containing protein 6), a key enzyme. This study reveals SETD6

Keywords:
InteractomeMass spectrometrySETD6

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • SETD6 (SET-domain-containing protein 6) is a mono-methyltransferase with known roles in methylating RelA and H2AZ.
  • Previous studies have identified novel SETD6 substrates using proteomic approaches.

Purpose of the Study:

  • To identify novel proteins that interact with SETD6.
  • To elucidate the broader functional network of SETD6 within human cells.

Main Methods:

  • Immunoprecipitation (IP) of SETD6 from K562 cell lysates.
  • Mass-spectrometry analysis to identify SETD6 binding proteins.
  • Bioinformatic analysis using the STRING database and Gene Ontology (GO) for network and pathway enrichment.

Main Results:

  • Identification of 115 new potential SETD6 binding candidates.
  • Mapping of the SETD6 interactome network.
  • Enrichment analysis revealed significant associations with metabolic processes, muscle contraction, and protein folding.

Conclusions:

  • The study expands the known interactome of SETD6, revealing new potential binding partners.
  • The identified protein network suggests novel roles for SETD6 in fundamental cellular processes including metabolism, muscle function, and protein homeostasis.
  • Further investigation into these interactions could uncover new therapeutic targets.