| Autor: |
Kerscher, Stefan, Albert, Susanne, Wucherpfennig, Doris, Heisenberg, Martin, Schneuwly, Stephan |
| Zdroj: |
Developmental Biology; April 1995, Vol. 168 Issue: 2 p613-626, 14p |
| Abstrakt: |
Glycosylation is an important mechanism for modulating the physicochemical and biological properties of proteins in a stage- and tissue-specific manner. The enzymology of this process is just beginning to be understood. Here we present the molecular analysis of mas-1(mannosidase-1), a Drosophilagene with significant homologies to mammalian and Saccharomyces cerevisiaeglycoprotein processing α1,2-mannosidases. An enhancer-trap P-element inserted upstream of mas-1leads to highly specific lacZ expression in the lobula plate giant neurons, cells that mediate the large-field optomotor response. This staining, however, seems to reflect only a small part of the complex expression pattern of the mas-1gene: Two promoters produce alternative transcripts that show individual spatial distributions during embryonic development, including a maternal contribution. Both transcripts code for type II transmembrane proteins which differ in their N-terminal parts. Null mutants in mas-1display defects in the embryonic PNS, in the wing, and in the adult eye. These findings illustrate that the processing of N-linked glycans plays a functional role in Drosophiladevelopment. There is, however, ample evidence for genetic and biochemical redundancy in the mannose-trimming steps of this pathway. |
| Databáze: |
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