Leveraging coevolutionary insights and AI-based structural modeling to unravel receptor-peptide ligand-binding mechanisms.
evolution
ligand
peptide
receptor
structure prediction
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
13 Aug 2024
13 Aug 2024
Historique:
medline:
6
8
2024
pubmed:
6
8
2024
entrez:
6
8
2024
Statut:
ppublish
Résumé
Secreted signaling peptides are central regulators of growth, development, and stress responses, but specific steps in the evolution of these peptides and their receptors are not well understood. Also, the molecular mechanisms of peptide-receptor binding are only known for a few examples, primarily owing to the limited availability of protein structural determination capabilities to few laboratories worldwide. Plants have evolved a multitude of secreted signaling peptides and corresponding transmembrane receptors. Stress-responsive SERINE RICH ENDOGENOUS PEPTIDES (SCOOPs) were recently identified. Bioactive SCOOPs are proteolytically processed by subtilases and are perceived by the leucine-rich repeat receptor kinase MALE DISCOVERER 1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) in the model plant
Identifiants
pubmed: 39106311
doi: 10.1073/pnas.2400862121
doi:
Substances chimiques
Arabidopsis Proteins
0
Ligands
0
Protein Serine-Threonine Kinases
EC 2.7.11.1
Peptides
0
At3g51550 protein, Arabidopsis
EC 2.7.-
Phosphotransferases
EC 2.7.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2400862121Subventions
Organisme : EC | European Research Council (ERC)
ID : 773153
Organisme : European Molecular Biology Organization (EMBO)
ID : 580-2022
Organisme : Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (SNF)
ID : 310030_204526
Déclaration de conflit d'intérêts
Competing interests statement:The authors declare no competing interest.