Drosophila fasciclin I, a neural cell adhesion molecule, has a phosphatidylinositol lipid membrane anchor that is developmentally regulated

Fasciclin I is a homophilic neural cell adhesion molecule which is regionally expressed on a subset of fasciculating axons in both the grasshopper and Drosophila embryo, suggesting a role in axonal recognition. It is also dynamically expressed on a variety of other embryonic tissues. Biochemical ana...

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Bibliographic Details
Published in:The Journal of biological chemistry 1990-09, Vol.265 (25), p.15104-15109
Main Authors: HORTSCH, M, GOODMAN, G. S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Antibodies, Monoclonal
Biological and medical sciences
Cell Adhesion Molecules, Neuronal - genetics
Cell Adhesion Molecules, Neuronal - isolation & purification
Cell Adhesion Molecules, Neuronal - metabolism
Cells, Cultured
Diptera
Drosophila - embryology
Drosophila - genetics
Drosophilidae
Embryo, Nonmammalian - physiology
fasciclin T
Fundamental and applied biological sciences. Psychology
Glycoproteins
Glycosylphosphatidylinositols
Grasshoppers - genetics
Molecular Sequence Data
neural cell adhesion molecule
phosphatidylinositol
Phosphatidylinositols - metabolism
Polysaccharides - metabolism
Proteins
Sequence Homology, Nucleic Acid
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Summary:Fasciclin I is a homophilic neural cell adhesion molecule which is regionally expressed on a subset of fasciculating axons in both the grasshopper and Drosophila embryo, suggesting a role in axonal recognition. It is also dynamically expressed on a variety of other embryonic tissues. Biochemical analysis of the fasciclin I glycoprotein from Drosophila embryonic membranes and Schneider 1 cells indicates that it is tightly associated with the lipid bilayer by a phosphatidylinositol lipid moiety. In Drosophila embryos a large fraction of fasciclin I protein has lost its membrane anchor. The ratio of this soluble form to the phosphatidylinositol-linked form changes during embryogenesis. We speculate that removal of the phosphatidylinositol lipid from the fasciclin I protein could be a mechanism to regulate its adhesive function.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)77229-3