ArticleMolecular membrane biology2011
The amino acids upstream of NH(2)-terminal dileucine motif play a role in regulating the intracellular sorting of the Class III transporters GLUT8 and GLUT12.
Article in Molecular membrane biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 12 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- The glucose transporter GLUT12, a new actor in obesity and cancer.Journal of physiology and biochemistry · 2025Review
- Identification of New Regulators of the Oocyte-to-Embryo Transition inG3 (Bethesda, Md.) · 2020Article
- Glucose transporters in adipose tissue, liver, and skeletal muscle in metabolic health and disease.Pflugers Archiv : European journal of physiology · 2020Review
- Structure, function and regulation of mammalian glucose transporters of the SLC2 family.Pflugers Archiv : European journal of physiology · 2020Review
- Glucose transporters in the small intestine in health and disease.Pflugers Archiv : European journal of physiology · 2020Review
- Glucose Transport and Transporters in the Endomembranes.International journal of molecular sciences · 2019Review
- The apical sorting signal for human GLUT9b resides in the N-terminus.Molecular and cellular biochemistry · 2013Article
- Hepatic expression and cellular distribution of the glucose transporter family.World journal of gastroenterology · 2012Review
- The SLC2 (GLUT) family of membrane transporters.Molecular aspects of medicineReview
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3 authors at 1 institution in 1 country.
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Abstract
The transport of glucose across cell membranes is mediated by a family of facilitative glucose transporters (GLUTs). The class III glucose transporters GLUT8 and GLUT12 both contain a similar [DE]XXXL[LI] dileucine sorting signal in their amino terminus. This type of dileucine motif facilitates protein trafficking to various organelles or to the plasma membrane via interactions with adaptor protein (AP) complexes. The [DE]XXXL[LI] motif in GLUT8 is thought to direct it to late endosomal/lysosomal compartments via its interactions with AP1 and AP2. Unlike GLUT8, the [DE]XXXL[LI] motif does not direct GLUT12 to a lysosomal compartment. Rather, GLUT12 resides in the Golgi network and at the plasma membrane. In a previous study, we found that exchanging the XXX (TQP) residues in GLUT8 with the corresponding residues in GLUT12 (GPN) resulted in a dramatic missorting of GLUT8 to the cell surface. We postulated that the XXX amino acids upstream of the dileucine motif in GLUT8 influence the degree of interaction between the [DE]XXXL[LI] motif and adaptor proteins. To further explore its trafficking mechanisms, we created mutant constructs to identify the role that each of the individual XXX amino acids has for regulating the intracellular sorting of GLUT8. Here we find that the XXX amino acids, specifically the position of a proline -2 from the dileucine residues, influence the affinity of APs for GLUT8 and GLUT12.
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