Centrosomes, functioning as microtubule organizing centers, are composed of a proteinaceous matrix of pericentriolar material (PCM) that surrounds a pair of centrioles.
Drosophila
Pericentrin (Pcnt)-like protein (PLP) is a key component of the centrosome that serves as a scaffold for PCM assembly. The disruption of
plp
in
Drosophila
results in embryonic lethality, while the deregulation of Pcnt in humans is associated with MOPD II and Trisomy 21.We recently found
plp
mRNA localizes to
Drosophila
embryonic centrosomes. While RNA is known to associate with centrosomes in diverse cell types, the elements required for
plp
mRNA localization to centrosomes remains completely unknown. Additionally, how
plp
translation is regulated to accommodate rapid cell divisions during early embryogenesis is unclear. RNA localization coupled with translational control is a conserved mechanism that functions in diverse cellular processes. Control of mRNA localization and translation is mediated by RNA-binding proteins (RBPs). We find PLP protein expression is specifically promoted by an RNA-binding protein, Orb, during embryogenesis; moreover,
plp
mRNA interacts with Orb. Importantly, we find overexpression of full-length PLP can rescue cell division defects and embryonic lethality caused by
orb
depletion. We aim to uncover the mechanisms underlying embryonic
plp
mRNA localization and function and how Orb regulates
plp
translation.