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

Chien-liang Glenn Lin, Irina Orlov, Alicia M. Ruggiero, Margaret Dykes-Hoberg, Andy Lee, Mandy Jackson and Jeffrey D. Rothstein ()
Additional contact information
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

Nature, 2001, vol. 410, issue 6824, 84-88

Abstract: 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.

Date: 2001
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/35065084 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:410:y:2001:i:6824:d:10.1038_35065084

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/35065084

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().