Identification of brain-specific angiogenesis inhibitor 2 as an interaction partner of glutaminase interacting protein.
Biochem Biophys Res Commun
; 411(4): 792-7, 2011 Aug 12.
Article
in En
| MEDLINE
| ID: mdl-21787750
ABSTRACT
The vast majority of physiological processes in living cells are mediated by protein-protein interactions often specified by particular protein sequence motifs. PDZ domains, composed of 80-100 amino acid residues, are an important class of interaction motif. Among the PDZ-containing proteins, glutaminase interacting protein (GIP), also known as Tax Interacting Protein TIP-1, is unique in being composed almost exclusively of a single PDZ domain. GIP has important roles in cellular signaling, protein scaffolding and modulation of tumor growth and interacts with a number of physiological partner proteins, including Glutaminase L, ß-Catenin, FAS, HTLV-1 Tax, HPV16 E6, Rhotekin and Kir 2.3. To identify the network of proteins that interact with GIP, a human fetal brain cDNA library was screened using a yeast two-hybrid assay with GIP as bait. We identified brain-specific angiogenesis inhibitor 2 (BAI2), a member of the adhesion-G protein-coupled receptors (GPCRs), as a new partner of GIP. BAI2 is expressed primarily in neurons, further expanding GIP cellular functions. The interaction between GIP and the carboxy-terminus of BAI2 was characterized using fluorescence, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy assays. These biophysical analyses support the interaction identified in the yeast two-hybrid assay. This is the first study reporting BAI2 as an interaction partner of GIP.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Intracellular Signaling Peptides and Proteins
/
Nerve Tissue Proteins
Type of study:
Diagnostic_studies
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2011
Document type:
Article
Affiliation country: