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Wild type and constitutively activated forms of the Drosophila Toll receptor have different patterns of N‐linked glycosylation
Author(s) -
Kubota Ken,
Keith Fionna J.,
Gay Nicholas J.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00428-c
Subject(s) - biology , glycosylation , receptor , microbiology and biotechnology , glycoprotein , schneider 2 cells , signal transduction , mutant , wild type , gene isoform , gene , biochemistry , rna , rna interference
Toll is a Drosophila membrane protein related in sequence to the mammalian platelet glycoprotein 1B and to the interleukin‐1 receptor. It mediates a signal transduction pathway leading to the development of dorsoventral polarity in the Drosophila embryo. In this paper we show that a constitutively activated mutant receptor, Toll10B, is processed into a distinct isoform of slower electrophoretic mobility when compared with the wild type molecule in both cell lines and the embryo. The wild type protein can also be processed into this form if over‐expressed but in the embryo is present as the smaller species. We show that the decrease in the mobility of Toll10B and over‐expressed wild type receptors is caused by altered patterns of N‐linked glycosylation and that both forms are secreted to the cell surface. On the basis of these results, we propose that the Toll10B receptor is unable to associate with a limiting co‐factor which when bound directly or indirectly masks supplementary N‐linked glycosylation sites.