The C‐terminus of human glutaminase L mediates association with PDZ domain‐containing proteins 1

FEBS Letters

Aledo, J.Carlos¹  Márquez, Javier¹  Olalla, Lucı́a¹  Bannenberg, Gerard¹ 

[1] Departamento de Biologı́a Molecular y Bioquı́mica, Laboratorio de Quı́mica de Proteı́nas, Facultad de Ciencias, Universidad de Málaga, 29071 Málaga, Spain

关键词: Human glutaminase;    Brain;    Two-hybrid;    PDZ protein;    Syntrophin;    PAG;    phosphate-activated glutaminase;    SNT;    α1-syntrophin;    GIP;    glutaminase-interacting protein;    GST;    glutathione S-transferase;    PDZ;    postsynaptic density protein PSD-95/SAP90;    Drosophila tumor suppressor protein DLG and tight junction protein ZO-1;   

DOI  :  10.1016/S0014-5793(00)02373-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown