Neutralization of the aspartic acid residue Asp-367, but not Asp-454, inhibits binding of Na+ to the glutamate-free form and cycling of the glutamate transporter EAAC1

Journal of Biological Chemistry

Volumn 281, Issue 15, 2006, Pages 10263-10272

  Tao, Zhen ^a   Zhang, Zhou ^a   Grewer, Christof ^a,b  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

^b NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CARBOXYLIC ACIDS; CELLS; CYTOLOGY; MUTAGENESIS;

GLUTAMATE TRANSLOCATION; GLUTAMATE-FREE TRANSPORTERS; MUTANT TRANSPORTER; TRANSMEMBRANE SEGMENTS;

BIOCHEMISTRY;

ASPARAGINE; ASPARTIC ACID; EXCITATORY AMINO ACID TRANSPORTER; GLUTAMIC ACID; ANION; EXCITATORY AMINO ACID TRANSPORTER 3; GLUTAMATE TRANSPORTER; ION; SLC1A1 PROTEIN, HUMAN; SODIUM;

AMINO ACID SUBSTITUTION; AMINO ACID TRANSPORT; ARTICLE; BINDING AFFINITY; BINDING COMPETITION; BINDING KINETICS; BINDING SITE; CONTROLLED STUDY; HUMAN; HUMAN CELL; MISSENSE MUTATION; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN TRANSPORT; SODIUM TRANSPORT; STEADY STATE; TRANSPORT KINETICS; AMINO ACID SEQUENCE; ANIMAL; BIOLOGICAL MODEL; CATALYSIS; CELL LINE; CELL MEMBRANE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; ELECTROPHYSIOLOGY; GENETIC TRANSFECTION; KINETICS; LASER; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHOTOLYSIS; RAT; SEQUENCE HOMOLOGY; TIME; TRANSPORT AT THE CELLULAR LEVEL;

AMINO ACID SEQUENCE; AMINO ACID TRANSPORT SYSTEM X-AG; ANIMALS; ANIONS; ASPARTIC ACID; BINDING SITES; BINDING, COMPETITIVE; BIOLOGICAL TRANSPORT; CATALYSIS; CELL LINE; CELL MEMBRANE; CLONING, MOLECULAR; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHYSIOLOGY; EXCITATORY AMINO ACID TRANSPORTER 3; GLUTAMIC ACID; HUMANS; IONS; KINETICS; LASERS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOTOLYSIS; PROTEIN BINDING; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM; TIME FACTORS; TRANSFECTION;

EID: 33744518437     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M510739200     Document Type: Article

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