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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-sy...

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Bibliographic Details
Published in:Insect molecular biology 2003-10, Vol.12 (5), p.427-432
Main Authors: Hansen, I.A, Gutsmann, V, Meyer, S.R, Scheller, K
Format: Article
Language:English
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Summary: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.
ISSN:0962-1075
1365-2583
DOI:10.1046/j.1365-2583.2003.00426.x