Disease relevance of Fas1

• All of the pioneering brain neurons express the cell adhesion molecule fasciclin I during initial axon outgrowth and fasciculation [1].

High impact information on Fas1

• Genetic analysis of a Drosophila neural cell adhesion molecule: interaction of fasciclin I and Abelson tyrosine kinase mutations [2].
• Drosophila fasciclin I is a homophilic cell adhesion molecule expressed in the developing embryo on the surface of a subset of fasciculating CNS axons, all PNS axons, and some nonneuronal cells [2].
• We have identified protein-null mutations in the fasciclin I (fas I) gene, and show that these mutants are viable and do not display gross defects in nervous system morphogenesis [2].
• Antibodies against Drosophila fasciclin I reveal that it is expressed on the surface of a subset of commissural axon pathways in the embryonic central nervous system and on all sensory axon pathways in the peripheral nervous system [3].
• The fasciclin I, II, and III glycoproteins are expressed on different subsets of axon bundles (fascicles) in insect embryos and are thus candidates for surface recognition molecules involved in growth cone guidance [3].

Biological context of Fas1

• One phenotype seen in fasII mutants and in animals mutant for both fasI and fasIII was extra branching within the axon projection pattern [4].
• Altered nerve terminal arborization and synaptic transmission in Drosophila mutants of cell adhesion molecule fasciclin I [5].

Anatomical context of Fas1

• 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 [6].
• Midline Fasciclin: a Drosophila Fasciclin-I-related membrane protein localized to the CNS midline cells and trachea [7].
• Algal-CAM is a protein with a three-domain structure: an N-terminal extensin-like domain characteristic for plant cell walls and two repeats with homology to fasciclin I, a cell adhesion molecule involved in the neuronal development of Drosophila [8].
• To facilitate structure-function studies, we have generated Chinese hamster ovary (CHO) cell lines expressing high levels of cell surface grasshopper and Drosophila fasciclin I [9].
• We also generated CHO and Drosophila S2 cell lines that produce a secreted form of fasciclin I [9].

Associations of Fas1 with chemical compounds

• Fasciclin I is a membrane-associated glycoprotein that is regionally expressed on a subset of fasciculating axons during neuronal development in insects; it is expressed on apposing cell surfaces, suggesting a role in specific cell adhesion [10].

Other interactions of Fas1

• A third artificial neuroglian protein form was constructed by substituting the neuroglian transmembrane segment and cytoplasmic domains with the glycosyl phosphatidylinositol attachment signal of the Drosophila fasciclin I protein [11].
• The midline fasciclin gene encodes a second Drosophila member of the Fasciclin I family [7].
• Drosophila fasciclin I is a novel homophilic adhesion molecule that along with fasciclin III can mediate cell sorting [10].
• Grasshopper fasciclin I released by phospholipase C cleavage was purified on an immunoaffinity column and single crystals were obtained that diffracted to approximately 5-A resolution [9].

Analytical, diagnostic and therapeutic context of Fas1

• Sequence analysis and neuronal expression of fasciclin I in grasshopper and Drosophila [3].
• Circular dichroism studies suggest that fasciclin I is primarily alpha-helical [9].
• Fasciclin I expressed in S2 cells contains significantly less carbohydrate than the protein expressed in CHO cells, and may therefore be more suitable for crystallization [9].

References