Science · 1990 · 881 citations · 30 references
Life SciencesMolecular BiologyNeuroscienceMolecular NeurobiologyMolecular NeuroscienceNeuropharmacologyGlutamatergic SignalingNeurotransmissionComplementary Dna (Cdna) CloningExcitatory Amino Acid TransportersGaba Transporter FunctionHydropathy AnalysisShared Antigenic DeterminantsTransmembrane DomainsTransmembrane Proteins
Hydropathy analysis indicates multiple transmembrane domains, but GAT‑1 shows no homology to known proteins. The cloned GAT‑1 cDNA encodes a 599‑amino‑acid, 67‑kDa GABA transporter that functions in Xenopus oocytes with high affinity, sodium‑ and chloride‑dependence, and pharmacological similarity to neuronal transporters, and represents a novel, previously uncharacterized family of transport molecules.
A complementary DNA clone (designated GAT-1) encoding a transporter for the neurotransmitter γ-aminobutyric acid (GABA) has been isolated from rat brain, and its functional properties have been examined in Xenopus oocytes. Oocytes injected with GAT-1 synthetic messenger RNA accumulated [ 3 H]GABA to levels above control values. The transporter encoded by GAT-1 has a high affinity for GABA, is sodium-and chloride-dependent, and is pharmacologically similar to neuronal GABA transporters. The GAT-1 protein shares antigenic determinants with a native rat brain GABA transporter. The nucleotide sequence of GAT-1 predicts a protein of 599 amino acids with a molecular weight of 67 kilodaltons. Hydropathy analysis of the deduced protein suggests multiple transmembrane regions, a feature shared by several cloned transporters; however, database searches indicate that GAT-1 is not homologous to any previously identified proteins. Therefore, GAT-1 appears to be a member of a previously uncharacterized family of transport molecules.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations