Sm. Bahri et al., THE DROSOPHILA BIFOCAL GENE ENCODES A NOVEL PROTEIN WHICH COLOCALIZESWITH ACTIN AND IS NECESSARY FOR PHOTORECEPTOR MORPHOGENESIS, Molecular and cellular biology, 17(9), 1997, pp. 5521-5529
Photoreceptor cells of the Drosophila compound eye begin to develop sp
ecialized membrane foldings at the apical surface in midpupation. The
microvillar structure ultimately forms the rhabdomere, an actin-rich l
ight-gathering organelle with a characteristic shape and morphology. I
n a P-element transposition screen, we isolated mutations in a gene, b
ifocal (bif), which is required for the development of normal rhabdome
res. The morphological defects seen in bif mutant animals, in which th
e distinct contact domains established by the newly formed rhabdomeres
are abnormal, first become apparent during midpupal development, The
later defects seen in the mutant adult R cells are more dramatic, with
the rhabdomeres enlarged, elongated, and frequently split, bif encode
s a novel putative protein of 1063 amino acids which is expressed in t
he embryo and the larval eye imaginal disc in a pattern identical to t
hat of F actin, During pupal development, Bif localizes to the base of
the filamentous actin associated with the forming rhabdomeres along o
ne side of the differentiating R cells. On the basis of its subcellula
r localization and loss-of-function phenotype, we discuss possible rol
es of Bif in photoreceptor morphogenesis.