The primary study on a novel protein binding to the death domain of the death receptor 4.
- Author:
Xiao-ling LI
1
;
Yan-xin LIU
;
Shi-lian LIU
;
De-xian ZHENG
Author Information
- Publication Type:Journal Article
- MeSH: Amino Acid Sequence; Apoptosis; Apoptosis Regulatory Proteins; Base Sequence; Carrier Proteins; biosynthesis; genetics; Cloning, Molecular; Humans; Membrane Glycoproteins; metabolism; Molecular Sequence Data; Protein Structure, Tertiary; Receptors, Formyl Peptide; metabolism; Receptors, Lipoxin; metabolism; Receptors, TNF-Related Apoptosis-Inducing Ligand; Receptors, Tumor Necrosis Factor; genetics; metabolism; Signal Transduction; TNF-Related Apoptosis-Inducing Ligand; Tumor Necrosis Factor-alpha; metabolism
- From: Acta Academiae Medicinae Sinicae 2002;24(3):310-314
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo clone and identify novel proteins binding to the death domain of the death receptor 4 (DR4).
METHODSThe yeast two-hybrid system was used for this study. Automatic sequencing was carried out for DNA sequencing. The sequence homology and the functional domains were analyzed by BLAST and the ScanProsite Tool softwares, respectively. Co-immunoprecipitate method was used to confirm human formyl peptide receptor-like 1 (FPRL1) binding specifically with DR4CD (the cytoplasmic domain of DR4) in HEK293T cells.
RESULTSTwo positive clones, named as pADB1 and pADB2, were obtained. BLAST searching showed that the homology of the insert sequence of pADB1 with the mRNA of FPRL1 was 97%. The insert of pADB2 shared no homology with any known peptides in GeneBank. Co-immunoprecipitate analysis further confirmed that FPRL1 could bind to DR4CD in vivo specifically.
CONCLUSIONSFPRL1 may associate with DR4CD in vivo specifically. The functional studies of FPRL1 in signaling pathway mediated by TNF-related apoptosis inducing ligand (TRAIL) are in active progress in our laboratory.
