The intracellular helical bundle of human glucose transporter GLUT4 is important for complex formation with ASPL.
ASPL
GLUT4
TUG
adipocyte
glucose transporters
trafficking
Journal
FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716
Informations de publication
Date de publication:
11 2023
11 2023
Historique:
revised:
06
09
2023
received:
18
08
2023
accepted:
19
09
2023
medline:
7
11
2023
pubmed:
21
9
2023
entrez:
21
9
2023
Statut:
ppublish
Résumé
Glucose transporters (GLUTs) are responsible for transporting hexose molecules across cellular membranes. In adipocytes, insulin stimulates glucose uptake by redistributing GLUT4 to the plasma membrane. In unstimulated adipose-like mouse cell lines, GLUT4 is known to be retained intracellularly by binding to TUG protein, while upon insulin stimulation, GLUT4 dissociates from TUG. Here, we report that the TUG homolog in human, ASPL, exerts similar properties, i.e., forms a complex with GLUT4. We describe the structural details of complex formation by combining biochemical assays with cross-linking mass spectrometry and computational modeling. Combined, the data suggest that the intracellular domain of GLUT4 binds to the helical lariat of ASPL and contributes to the regulation of GLUT4 trafficking by cooperative binding.
Identifiants
pubmed: 37731227
doi: 10.1002/2211-5463.13709
pmc: PMC10626271
doi:
Substances chimiques
Carrier Proteins
0
Glucose
IY9XDZ35W2
Glucose Transport Proteins, Facilitative
0
Intracellular Signaling Peptides and Proteins
0
Insulin
0
Banques de données
PDB
['7WSM', '5IFS']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
2094-2107Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK129466
Pays : United States
Informations de copyright
© 2023 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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