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Modulation of the neuronal glutamate transporter EAAC1 by the interacting protein GTRAP3-18

Author

Listed:
  • Chien-liang Glenn Lin

    (Johns Hopkins University, Meyer 6-109)

  • Irina Orlov

    (Johns Hopkins University, Meyer 6-109)

  • Alicia M. Ruggiero

    (Johns Hopkins University, Meyer 6-109)

  • Margaret Dykes-Hoberg

    (Johns Hopkins University, Meyer 6-109)

  • Andy Lee

    (Johns Hopkins University, Meyer 6-109)

  • Mandy Jackson

    (Johns Hopkins University, Meyer 6-109)

  • Jeffrey D. Rothstein

    (Johns Hopkins University, Meyer 6-109)

Abstract

Excitatory amino-acid carrier 1 (EAAC1) is a high-affinity Na+-dependent l-glutamate/d, l-aspartate cell-membrane transport protein1. It is expressed in brain as well as several non-nervous tissues. In brain, EAAC1 is the primary neuronal glutamate transporter2,3. It has a polarized distribution in cells and mainly functions perisynaptically to transport glutamate from the extracellular environment2,3,4. In the kidney it is involved in renal acidic amino-acid re-absorption and amino-acid metabolism5,6,7. Here we describe the identification and characterization of an EAAC1-associated protein, GTRAP3-18. Like EAAC1, GTRAP3-18 is expressed in numerous tissues8,9. It localizes to the cell membrane and cytoplasm, and specifically interacts with carboxy-terminal intracellular domain of EAAC1. Increasing the expression of GTRAP3-18 in cells reduces EAAC1-mediated glutamate transport by lowering substrate affinity. The expression of GTRAP3-18 can be upregulated by retinoic acid, which results in a specific reduction of EAAC1-mediated glutamate transport. These studies show that glutamate transport proteins can be regulated potently and that GTRAP can modulate the transport functions ascribed to EAAC1. GTRAP3-18 may be important in regulating the metabolic function of EAAC1.

Suggested Citation

  • Chien-liang Glenn Lin & Irina Orlov & Alicia M. Ruggiero & Margaret Dykes-Hoberg & Andy Lee & Mandy Jackson & Jeffrey D. Rothstein, 2001. "Modulation of the neuronal glutamate transporter EAAC1 by the interacting protein GTRAP3-18," Nature, Nature, vol. 410(6824), pages 84-88, March.
    • Handle: RePEc:nat:nature:v:410:y:2001:i:6824:d:10.1038_35065084
    DOI: 10.1038/35065084
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    Cited by:

    1. Weidong Zhang & Ayako Miura & Md Moin Abu Saleh & Koichiro Shimizu & Yuichiro Mita & Ryota Tanida & Satoshi Hirako & Seiji Shioda & Valery Gmyr & Julie Kerr-Conte & Francois Pattou & Chunhuan Jin & Yo, 2023. "The NERP-4–SNAT2 axis regulates pancreatic β-cell maintenance and function," Nature Communications, Nature, vol. 14(1), pages 1-21, December.

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