Dn. Cox et al., Bazooka and atypical protein kinase C are required to regulate oocyte differentiation in the Drosophila ovary, P NAS US, 98(25), 2001, pp. 14475-14480
Citations number
41
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
The par genes, identified by their role in the establishment of anterior-po
sterior polarity in the Caenorhabditis elegans zygote, subsequently have be
en shown to regulate cellular polarity in diverse cell types by means of an
evolutionarily conserved protein complex including PAR-3, PAR-6, and atypi
cal protein kinase C (aPKC). The Drosophila homologs of par-1, par-3 (bazoo
ka, baz), par-6 (DmPar-6), and pkc-3 (Drosophila aPKC, DaPKC) each are know
n to play conserved roles in the generation of cell polarity in the germ li
ne as well as in epithelial and neural precursor cells within the embryo. i
n light of this functional conservation, we examined the potential role of
baz and DaPKC in the regulation of oocyte polarity. Our analyses reveal ger
m-line autonomous roles for baz and DaPKC in the establishment of initial a
nterior-posterior polarity within germ-line cysts and maintenance of oocyte
cell fate. Germ-line clonal analyses indicate both proteins are essential
for two key aspects of oocyte determination: the posterior translocation of
oocyte specification factors and the posterior establishment of the microt
ubule organizing center within the presumptive oocyte. We demonstrate BAZ a
nd DaPKC colocalize to belt-like structures between germarial cyst cells. H
owever, in contrast to their regulatory relationship in the Drosophila and
C. elegans embryos, these proteins are not mutually dependent for their ger
m-line localization, nor is either protein specifically required for PAR-1
localization to the fusome. Therefore, whereas BAZ, DaPKC, and PAR-1 are fu
nctionally conserved in establishing oocyte polarity, the regulatory relati
onships among these genes are not well conserved, indicating these molecule
s function differently in different cellular contexts.