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Uncovering domain motif interactions using high-throughput protein-protein interaction detection methods.
Idrees, Sobia; Paudel, Keshav Raj; Sadaf, Tayyaba; Hansbro, Philip M.
Affiliation
  • Idrees S; School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, Australia.
  • Paudel KR; Centre for Inflammation, Centenary Institute and Faculty of Science, School of Life Sciences, University of Technology Sydney, Australia.
  • Sadaf T; Centre for Inflammation, Centenary Institute and Faculty of Science, School of Life Sciences, University of Technology Sydney, Australia.
  • Hansbro PM; Centre for Inflammation, Centenary Institute and Faculty of Science, School of Life Sciences, University of Technology Sydney, Australia.
FEBS Lett ; 598(7): 725-742, 2024 Apr.
Article de En | MEDLINE | ID: mdl-38439692
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.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Protéines / Cartographie d'interactions entre protéines Langue: En Journal: FEBS Lett Année: 2024 Type de document: Article Pays d'affiliation: Australie Pays de publication: Royaume-Uni

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Protéines / Cartographie d'interactions entre protéines Langue: En Journal: FEBS Lett Année: 2024 Type de document: Article Pays d'affiliation: Australie Pays de publication: Royaume-Uni