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Functional dissection of the hexamerin receptor and its ligand arylphorin in the blowfly Calliphora vicina
Author(s) -
Hansen I. A.,
Gutsmann V.,
Meyer S. R.,
Scheller K.
Publication year - 2003
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.2003.00426.x
Subject(s) - biology , ligand (biochemistry) , receptor , biochemistry
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.