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Research Article

Alternative Splicing and Cleavage of GLUT8

Caroline M. Alexander, Joshua A. Martin, Elias Oxman, Ildiko Kasza, Katherine A. Senn, Heidi Dvinge
Caroline M. Alexander
aMcArdle Laboratory for Cancer Research, School of Medicine and Public Health, University of Wisconsin—Madison, Madison, Wisconsin, USA
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  • ORCID record for Caroline M. Alexander
Joshua A. Martin
aMcArdle Laboratory for Cancer Research, School of Medicine and Public Health, University of Wisconsin—Madison, Madison, Wisconsin, USA
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Elias Oxman
aMcArdle Laboratory for Cancer Research, School of Medicine and Public Health, University of Wisconsin—Madison, Madison, Wisconsin, USA
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Ildiko Kasza
aMcArdle Laboratory for Cancer Research, School of Medicine and Public Health, University of Wisconsin—Madison, Madison, Wisconsin, USA
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Katherine A. Senn
bDepartment of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin—Madison, Madison, Wisconsin, USA
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Heidi Dvinge
bDepartment of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin—Madison, Madison, Wisconsin, USA
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DOI: 10.1128/MCB.00480-20
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ABSTRACT

The GLUT (SLC2) family of membrane-associated transporters are described as glucose transporters. However, this family is divided into three classes and, though the regulated transporter activity of class I proteins is becoming better understood, class III protein functions continue to be obscure. We have cataloged the relative expression and splicing of SLC2 mRNA isomers in tumors and normal tissues, with a focus on breast tumors and cell lines. mRNA for the class III protein GLUT8 is the predominant SLC2 species expressed alongside GLUT1 in many tissues, but GLUT8 mRNA exists mostly as an untranslated splice form in tumors. We confirm that GLUT8 is not presented at the cell surface and does not transport glucose directly. However, we reveal a lysosome-dependent reaction that cleaves the GLUT8 protein and releases the carboxy-terminal peptide to a separate vesicle population. Given the localization of GLUT8 at a major metabolic hub (the late endosomal/lysosomal interface) and its regulated cleavage reaction, we evaluated TXNIP-mediated hexosamine homeostasis and speculate that GLUT8 may function as a sensory component of this reaction.

FOOTNOTES

    • Received 10 September 2020.
    • Accepted 1 October 2020.
    • Accepted manuscript posted online 19 October 2020.
  • Supplemental material is available online only.

  • Copyright © 2020 American Society for Microbiology.

All Rights Reserved.

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Alternative Splicing and Cleavage of GLUT8
Caroline M. Alexander, Joshua A. Martin, Elias Oxman, Ildiko Kasza, Katherine A. Senn, Heidi Dvinge
Molecular and Cellular Biology Dec 2020, 41 (1) e00480-20; DOI: 10.1128/MCB.00480-20

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Alternative Splicing and Cleavage of GLUT8
Caroline M. Alexander, Joshua A. Martin, Elias Oxman, Ildiko Kasza, Katherine A. Senn, Heidi Dvinge
Molecular and Cellular Biology Dec 2020, 41 (1) e00480-20; DOI: 10.1128/MCB.00480-20
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KEYWORDS

GLUT8
SLC2
TXNIP
alternative splicing
breast cancer
chromophobe renal cell carcinoma
cleavage
glucose transport
late endosomal-lysosomal boundary
metabolic sensor

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