Abstract
Targeting proteins to regions where they are required is essential for proper development of organisms. For achievement of this, subcellular mRNA localization is one of the critical mechanisms. Subcellular mRNA localization is an evolutionarily conserved phenomenon from E. coli to human and contributes to limiting the regions at which its products function and efficiently supplies substrates for protein translation. During early Drosophila embryogenesis, while 71% of the 3370 mRNAs analyzed have shown prominent subcellular localization, the underlying molecular mechanisms have not been elucidated. Here, we reveal that anillin mRNA, one of the localized mRNAs in early Drosophila embryo, localizes to the tip of the pseudo-cleavage furrow in the Drosophila syncytial blastoderm using in situ hybridization combined with immunohistochemistry. Localization analyses with transgenic fly lines carrying a series of deletion mRNAs indicate that this localization is dependent on its own nascent polypeptides including the actin binding domain (ABD). In addition to the mRNA localization, it is revealed that the pleckstrin homology (PH) domain of Anillin protein is also required for its proper localization. Thus, we indicate that the precise localization of Anillin protein is tightly regulated by the ABD on the nascent polypeptide and PH domain in the Drosophila syncytial blastoderm.
Highlights
In early Drosophila embryogenesis, the first thirteen nuclear divisions occur without accompanying cytokinesis[1]
These findings strongly suggest that anillin mRNA localizes to the pseudo-cleavage furrow (PCF)
In order to investigate more precisely whether anillin mRNA localizes to the PCF, we performed in situ hybridization combined with immunostaining with anti-discs large IgG, a plasma membrane and PCF marker
Summary
In early Drosophila embryogenesis, the first thirteen nuclear divisions occur without accompanying cytokinesis[1]. In order to prevent the collision of neighboring mitotic spindles, a transient membrane invagination called the pseudo-cleavage furrow (PCF) or metaphase furrow occurs between nuclei[2,3]. This furrow progressively ingresses from prophase to metaphase, and starts to retract at anaphase (Fig. 1A–E)[4]. The Anillin protein is one of the main components in the cleavage furrow and functions as a scaffold protein to maintain the contractile ring during cytokinesis and localizes to the PCF in the syncytial blastoderm with strong accumulation at the tip of the PCF7. In addition to the mRNA localization, the pleckstrin homology domain of Anillin protein is required for its proper localization at the tip of the PCF in the syncytial blastoderm
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