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The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins.

FEBS letters | Jan 19, 2001

http://www.ncbi.nlm.nih.gov/pubmed/11163757

The enzyme glutaminase in brain is responsible for the synthesis of neurotransmitter glutamate. We used the two-hybrid genetic selection system in yeast to look for interactors of glutaminase in human brain. We have identified two proteins containing PDZ domains, alpha1-syntrophin and a glutaminase-interacting protein, named GIP, that showed association with human glutaminase L, as deduced from specificity test of the two-hybrid system. The complete GIP cDNA clone has 1315 nucleotides with a 372-base open reading frame encoding a 124-amino acids protein. Glutaminase associates with both PDZ proteins through its C-terminal end; mutagenesis of single amino acids revealed the sequence -ESXV as essential for the interaction. These data suggest the possibility that PDZ domain-containing proteins are involved in the regulation of glutaminase in brain.

Pubmed ID: 11163757 RIS Download

Mesh terms: Amino Acid Sequence | Base Sequence | Binding Sites | Brain | Calcium-Binding Proteins | Glutaminase | Humans | Intracellular Signaling Peptides and Proteins | Isoenzymes | Membrane Proteins | Molecular Sequence Data | Muscle Proteins | Mutation | Neurotransmitter Agents | Protein Binding | Protein Structure, Tertiary | Sequence Alignment | Two-Hybrid System Techniques

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