Functional dissection of the hexamerin receptor and its ligand arylphorin in the blowfly Calliphora vicina.
The process of receptor-mediated uptake of hexamerin storage proteins from insect haemolymph by fat body cells is a unique feature of the class Insecta. We identified the binding domains of the hexamerin receptor and the hexamerin ligand arylphorin in the blowfly, by means of the yeast-two-hybrid-system. The receptor-binding domain of arylphorin was located within domain 3 of the arylphorin monomer. The ligand-binding domain of the hexamerin receptor was mapped to the extreme N-terminus of the receptor. The binding domains identified exhibit no similarity to any functional protein domains known to date. Additionally, we identified two previously unknown protein-interactors of the hexamerin receptor. The results of this study provide further insights regarding the mechanism of the receptor-mediated endocytosis of storage proteins in insects.
Hansen
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IA
Department of Cell and Developmental Biology, Biocentre of the University, Wuerzburg, Germany. immoh@citrus.ucr.edu
Gutsmann
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V
Meyer
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SR
Scheller
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K
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry*; D017931:DNA Primers; D004175:Diptera / Q000378:metabolism*; D005822:Genetic Vectors / Q000235:genetics; D006023:Glycoproteins / Q000737:chemistry*; D019476:Insect Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010957:Plasmids / Q000235:genetics; D011487:Protein Conformation; D016415:Sequence Alignment; D020798:Two-Hybrid System Techniques; D015003:Yeasts / Q000378:metabolism
D002352:Carrier Proteins; D017931:DNA Primers; D006023:Glycoproteins; D019476:Insect Proteins; C092382:arylphorin-binding proteins, insect; C041137:storage proteins, Insecta