A Module for Analyzing Interactomes via APEX-MS Integrated into PatternLab for Proteomics

J Am Soc Mass Spectrom. 2024 May 1;35(5):1055-1058. doi: 10.1021/jasms.3c00382. Epub 2024 Apr 12.

Abstract

Proximity labeling techniques, such as APEX-MS, provide valuable insights into proximal interactome mapping; however, the verification of biotinylated peptides is not straightforward. With this as motivation, we present a new module integrated into PatternLab for proteomics to enable APEX-MS data interpretation by targeting diagnostic fragment ions associated with APEX modifications. We reanalyzed a previously published APEX-MS data set and report a significant number of biotinylated peptides and, consequently, a confident set of proximal proteins. As the module is part of the widely adopted PatternLab for proteomics software suite, it offers users a comprehensive, easy, and integrated solution for data analysis. Given the broad utility of the APEX-MS technique in various biological contexts, we anticipate that our module will be a valuable asset to researchers, facilitating and enhancing interactome studies. PatternLab's APEX, including a usage protocol, is available at http://patternlabforproteomics.org/apex.

Keywords: APEX-MS; PatternLab for proteomics; ascorbate peroxidase; interactomes; protein−protein interactions.

MeSH terms

  • Biotinylation
  • Humans
  • Mass Spectrometry / methods
  • Peptides / analysis
  • Peptides / chemistry
  • Peptides / metabolism
  • Protein Interaction Mapping / methods
  • Proteomics* / methods
  • Software*

Substances

  • Peptides