Skip to Content
Merck
  • The intracellular helical bundle of human glucose transporter GLUT4 is important for complex formation with ASPL.

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

FEBS open bio (2023-09-21)
Peng Huang, Hannah Åbacka, Daniel Varela, Raminta Venskutonytė, Lotta Happonen, Jonathan S Bogan, Pontus Gourdon, Mahmood R Amiry-Moghaddam, Ingmar André, Karin Lindkvist-Petersson
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Monoclonal Anti-ASPSCR1 antibody produced in mouse, clone 3D10-1D11, purified immunoglobulin, buffered aqueous solution