Loading…
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...
Saved in:
Published in: | Insect molecular biology 2003-10, Vol.12 (5), p.427-432 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
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 |