The intracellular helical bundle of human glucose transporter GLUT4 is important for complex formation with ASPL

Peng Huang, Hannah Åbacka, Daniel Varela, Raminta Venskutonytė, Lotta Happonen, Jonathan S. Bogan, Pontus Gourdon, Mahmood R. Amiry-Moghaddam, Ingmar André, Karin Lindkvist-Petersson

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

Sammanfattning

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.

Originalspråkengelska
Sidor (från-till)2094-2107
TidskriftFEBS Open Bio
Volym13
Nummer11
Tidigt onlinedatum2023
DOI
StatusPublished - 2023

Bibliografisk information

Publisher Copyright:
© 2023 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

Ämnesklassifikation (UKÄ)

  • Biokemi och molekylärbiologi

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