The intracellular helical bundle of human glucose transporter GLUT4 is important for complex formation with ASPL.
JSON
Huang P, Åbacka H, Varela D, Venskutonytė R, Happonen L, Bogan JS, Gourdon P, Amiry-Moghaddam MR, André I, Lindkvist-Petersson K
FEBS Open Bio 13 (11) 2094-2107 [2023-11-00; online 2023-09-28]
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.
Structural Proteomics [Collaborative]
PubMed 37731227
DOI 10.1002/2211-5463.13709
Crossref 10.1002/2211-5463.13709