
To clone and identify novel proteins binding to the death domain of the death receptor 4 (DR4).The 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.Two 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.FPRL1 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.
Membrane Glycoproteins, Base Sequence, Tumor Necrosis Factor-alpha, Molecular Sequence Data, Apoptosis, Receptors, Formyl Peptide, Receptors, Tumor Necrosis Factor, Protein Structure, Tertiary, TNF-Related Apoptosis-Inducing Ligand, Receptors, TNF-Related Apoptosis-Inducing Ligand, Humans, Amino Acid Sequence, Cloning, Molecular, Receptors, Lipoxin, Apoptosis Regulatory Proteins, Carrier Proteins, Signal Transduction
Membrane Glycoproteins, Base Sequence, Tumor Necrosis Factor-alpha, Molecular Sequence Data, Apoptosis, Receptors, Formyl Peptide, Receptors, Tumor Necrosis Factor, Protein Structure, Tertiary, TNF-Related Apoptosis-Inducing Ligand, Receptors, TNF-Related Apoptosis-Inducing Ligand, Humans, Amino Acid Sequence, Cloning, Molecular, Receptors, Lipoxin, Apoptosis Regulatory Proteins, Carrier Proteins, Signal Transduction
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