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

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)2094-2107
JournalFEBS Open Bio
Volume13
Issue number11
Early online date2023
DOIs
Publication statusPublished - 2023

Subject classification (UKÄ)

  • Biochemistry and Molecular Biology

Free keywords

  • adipocyte
  • ASPL
  • glucose transporters
  • GLUT4
  • trafficking
  • TUG

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