Wild type and constitutively activated forms of the Drosophila Toll receptor have different patterns of N-linked glycosylation

摘要: Toll is a Drosophila membrane protein related in sequence to the mammalian platelet glycoprotein 1B and interleukin-1 receptor. It mediates signal transduction pathway leading development of dorsoventral polarity embryo. In this paper we show that constitutively activated mutant receptor, Toll10B, processed into distinct isoform slower electrophoretic mobility when compared with wild type molecule both cell lines The can also be form if over-expressed but embryo present as smaller species. We decrease Toll10B receptors caused by altered patterns N-linked glycosylation forms are secreted surface. On basis these results, propose receptor unable associate limiting co-factor which bound directly or indirectly masks supplementary sites.