(Hardy, 2005.6.1)

(Hardy, 2005.6.1)

(Ryder, 2004.4.26)

(Hardy, 2005.6.1)

(Caldwell et al., 2007)

(Hardy, 2005.6.1)

(Marygold, 2005.1.19)

(Marygold, 2005.1.19)

(Marygold, 2005.1.19)

(Marygold, 2005.1.19)

monoclonal antibody

(Bajpai et al., 2004, Gaziova et al., 2004)

monoclonal

(Schulz et al., 2004)

Not required for viability.

(Marygold, 2005.1.19)

Proper targetting of pck gene product to the pleated septate junctions in the tracheal system depends on Nrx-IV and cora but not Fas3.

(Behr et al., 2003)

Fas3 protein mediates synaptic target recognition through homophilic interaction.

(Kose et al., 1997)

Some of the proteins of apico-lateral junctions are required both for apico-basal cell polarity and for the signalling mechanisms controlling cell proliferation, whereas others are required more specifically in cell-cell signalling.

(Woods et al., 1997)

The primary target genes of Egfr are pnt, vnd and Fas3, these are induced in different ectodermal domains. Secondary target genes oc, argos and trn are activated by pnt in response to Egfr signalling. The proper induction of these genes requires the concomitant inactivation of aop, mediated by Egfr signalling.

(Gabay et al., 1996)

Fas3 acts as a synaptic target recognition molecule for motor neuron RP3, and the absence of Fas3 can be compensated for by other molecules.

(Chiba et al., 1995)

Regions important for homophilic specificity are defined and the crystal structure determined.

(Strong et al., 1994)

In pros mutants, where innervation of muscles fails, connectin and Fas3 are expressed on muscle surface begins in same developmental pattern as in wild type. However Fas3 expression declines towards the end of embryogenesis, whereas it persists in wild type.

(Broadie and Bate, 1993)

The phenotypes of Fas1, Fas2, Fas3 and nac mutants were analysed in the developing wing: the axon tracts in the CNS for the most part remain unaltered, and none of the phenotypes are 100% penetrant, indicating a fine-tuning role for these molecules in both the PNS and CNS.

(Whitlock, 1993)

Fas3, mys, disco, zip, l(2)gl, N and Egfr mutants show an additive phenotype in combination with Fas1^TE89Da.

(Elkins et al., 1990)

Analysis of Fas3 localisation suggest that the protein plays a role in growth cone guidance.

(Snow et al., 1989)

Identified by screening a cDNA expression library with monoclonal antibodies directed against embryonic CNS and shown to identify proteins expressed on the cell surface of a restricted subset of cells of the embryo, including specific cells of the developing central nervous system. Monoclonal-antibody staining reveals a complex sequence of temporal and spatial expression of Fas3. It is expressed on segmentally repeated patches of cells during neurogenesis and outside the developing CNS on segmentally repeated stripes in the epidermis at the segmental grooves, on patches of epithelial cells near the stomodeal and proctodeal invaginations, on the visceral but not the somatic mesoderm, and on the luminal surface of the salivary gland epithelium; expression is highest where fasciclin-III-positive cells contact one another. After germ-band extension transiently expressed on segmentally repeated patches of neuroepithelial cells and specific underlying neuronal lineages; by the end of germ band retraction fasciclin-III is expressed in repeated stripes across all body segments. At hour 12 fasciclin is detected on a subset of three axon bundles (fascicles) in the anterior commissure and two in the posterior commissure of each segment; generally, however it's not expressed on the axons of these neurons that exit CNS, specifically on the longitudinal fascicles. Expression of Fas3 in transfected cultured cells promotes their adhesion to each other, but not to nonexpressing cells (Snow, Bieber and Goodman, 1989). The monoclonal antibodies used in the isolation of fasciclin identify four closely related membrane glycoproteins of 80, 66, 59 and 46kD molecular weight; all depend on the presence of Fas3⁺ for their presence.