The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate.
IDP
JAK2
NMR
human
integrative structural biology
molecular biophysics
simulation
single pass receptor
structural biology
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
26 05 2023
26 05 2023
Historique:
received:
02
11
2022
accepted:
24
05
2023
medline:
14
6
2023
pubmed:
26
5
2023
entrez:
26
5
2023
Statut:
epublish
Résumé
Class 1 cytokine receptors transmit signals through the membrane by a single transmembrane helix to an intrinsically disordered cytoplasmic domain that lacks kinase activity. While specific binding to phosphoinositides has been reported for the prolactin receptor (PRLR), the role of lipids in PRLR signaling is unclear. Using an integrative approach combining nuclear magnetic resonance spectroscopy, cellular signaling experiments, computational modeling, and simulation, we demonstrate co-structure formation of the disordered intracellular domain of the human PRLR, the membrane constituent phosphoinositide-4,5-bisphosphate (PI(4,5)P
Identifiants
pubmed: 37232489
doi: 10.7554/eLife.84645
pii: 84645
pmc: PMC10260020
doi:
pii:
Substances chimiques
Carrier Proteins
0
Janus Kinase 2
EC 2.7.10.2
Prolactin
9002-62-4
Receptors, Prolactin
0
STAT5 Transcription Factor
0
JAK2 protein, human
EC 2.7.10.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2023, Araya-Secchi et al.
Déclaration de conflit d'intérêts
RA, KB, PS, AP, GH, KL, SP, LA, BK No competing interests declared
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