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Fig. 4. Fak56 is not required for localization of components of adhesion complexes at muscle attachment sites. Wild-type and Fak56^CG1 embryos were immunostained with antibodies recognizing proteins previously known to localize at muscle attachment sites. Three distinct protein components are shown, representing extracellular, transmembrane and intracellular components of the muscle attachment site. Wild-type and Fak56^CG1 embryos were stained with anti-Tiggrin (A), anti-ßPS integrin (B), and anti-Talin (C) antibodies (green). Both genotypes showed wild-type localization at muscle attachment sites (arrowheads). All embryos were double-stained with Rhodamine-Phalloidin (red) to visualize actin filaments and muscle attachment sites. Low magnification is shown in (i) and (v). High magnifications of the muscle attachment sites are shown in (ii)-(iv) and (vi)-(viii). (D) Fak56 is not required for migration of the primordial midgut cells. The enhancer trap insertion line 258 was used to study the migration of the primordial midgut cells in Fak56 mutant embryos. The endodermal midgut arises from two primordia, the anterior midgut (AMG) and the posterior migut (PMG) primordium [(i) and (v), stage 10 embryos]. To form the midgut, these extend toward each other during stages 11 and 13 [(ii), (iii), (vi) and (vii)] and fuse laterally on both sides of the yolk, at stage 14 [(iv) and (viii)]. No obvious defects in the migration of primordial midgut cells could be observed in Fak56^CG1 mutant embryos, when compared with wild-type controls.

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