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The C‐terminus of human glutaminase L mediates association with PDZ domain‐containing proteins 1
Author(s) -
Olalla Lucı́a,
Aledo J.Carlos,
Bannenberg Gerard,
Márquez Javier
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02373-5
Subject(s) - pdz domain , glutaminase , amino acid , biochemistry , biology , complementary dna , mutagenesis , open reading frame , peptide sequence , microbiology and biotechnology , chemistry , glutamine , mutation , gene
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, α1‐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.