Uncovering domain motif interactions using high-throughput protein-protein interaction detection methods

FEBS Lett. 2024 Apr;598(7):725-742. doi: 10.1002/1873-3468.14841. Epub 2024 Mar 5.

Abstract

Protein-protein interactions (PPIs) are often mediated by short linear motifs (SLiMs) in one protein and domain in another, known as domain-motif interactions (DMIs). During the past decade, SLiMs have been studied to find their role in cellular functions such as post-translational modifications, regulatory processes, protein scaffolding, cell cycle progression, cell adhesion, cell signalling and substrate selection for proteasomal degradation. This review provides a comprehensive overview of the current PPI detection techniques and resources, focusing on their relevance to capturing interactions mediated by SLiMs. We also address the challenges associated with capturing DMIs. Moreover, a case study analysing the BioGrid database as a source of DMI prediction revealed significant known DMI enrichment in different PPI detection methods. Overall, it can be said that current high-throughput PPI detection methods can be a reliable source for predicting DMIs.

Keywords: PPI databases; domain–motif interactions; high‐throughput methods; protein–protein interactions.

Publication types

  • Review

MeSH terms

  • Databases, Protein
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping*
  • Proteins* / metabolism

Substances

  • Proteins