ArticleThe FEBS journal2009
Lysosomal localization of GLUT8 in the testis--the EXXXLL motif of GLUT8 is sufficient for its intracellular sorting via AP1- and AP2-mediated interaction.
Article in The FEBS journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Crosstalk between TM4SF5 and GLUT8 regulates fructose metabolism in hepatic steatosis.Molecular metabolism · 2022Article
- Genome-wide analysis in Drosophila reveals diet-by-gene interactions and uncovers diet-responsive genes.G3 (Bethesda, Md.) · 2021Article
- Impact of liver-specific GLUT8 silencing on fructose-induced inflammation and omega oxidation.iScience · 2021Article
- Alternative Splicing and Cleavage of GLUT8.Molecular and cellular biology · 2020Article
- AP-2 reduces amyloidogenesis by promoting BACE1 trafficking and degradation in neurons.EMBO reports · 2020Article
- GLUT1 and GLUT8 support lactose synthesis in Golgi of murine mammary epithelial cells.Journal of physiology and biochemistry · 2019Article
- In silico analyses of protein glycosylating genes in the helminth Fasciola hepatica (liver fluke) predict protein-linked glycan simplicity and reveal temporally-dynamic expression profiles.Scientific reports · 2018Article
- Humanin (HN) and glucose transporter 8 (GLUT8) in pregnancies complicated by intrauterine growth restriction.PloS one · 2018Article
- SLC2A8 (GLUT8) is a mammalian trehalose transporter required for trehalose-induced autophagy.Scientific reports · 2016Article
- Slc2a8 deficiency in mice results in reproductive and growth impairments.Biology of reproduction · 2012Article
- 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.Molecular membrane biology · 2011Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The class III sugar transport facilitator GLUT8 co-localizes with the lysosomal protein LAMP1 in heterologous expression systems. GLUT8 carries a [D/E]XXXL[L/I]-type dileucine sorting signal that has been postulated to retain the protein in an endosomal/lysosomal compartment via interactions with clathrin adaptor protein (AP) complexes. However, contradictory findings have been described regarding the subcellular localization of the endogenous GLUT8 and the adaptor proteins that interact with its dileucine motif. Here we demonstrate that endogenous GLUT8 is localized in a late endosomal/lysosomal compartment of spermatocytes and spermatids, and that the adaptor complexes AP1 and AP2, but not AP3 or AP4, interact with its N-terminal intracellular domain (NICD). In addition, fusion of the GLUT8 NICD to the tailless lumenal domain of the IL-2 receptor alpha chain (TAC) protein (interleukin-2 receptor a chain) targeted the protein to intracellular membranes, indicating that its N-terminal dileucine signal is sufficient for endosomal/lysosomal targeting of the transporter. The localization and targeting of GLUT8 show striking similarities to sorting mechanisms reported for lysosomal proteins. Therefore, we suggest a potential role for GLUT8 in the so far unexplored substrate transport across intracellular membranes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.