Divisions that generate one neuronal lineage-committed and one self-renewing cell maintain the balance of proliferation and differentiation for the generation of neuronal diversity. The asymmetric inheritance of apical domains and components of the cell division machinery has been implicated in this process, and might involve interactions with cell fate determinants in regulatory feedback loops of an as yet unknown nature. Here, we report the dynamics of Anillin – an essential F-actin regulator and furrow component – and its contribution to progenitor cell divisions in the developing zebrafish retina. We find that asymmetrically dividing retinal ganglion cell progenitors position the Anillin-rich midbody at the apical domain of the differentiating daughter. anillin hypomorphic conditions disrupt asymmetric apical domain inheritance and affect daughter cell fate. Consequently, the retinal cell type composition is profoundly affected, such that the ganglion cell layer is dramatically expanded. This study provides the first in vivo evidence for the requirement of Anillin during asymmetric neurogenic divisions. It also provides insights into a reciprocal regulation between Anillin and the ganglion cell fate determinant Ath5, suggesting a mechanism whereby the balance of proliferation and differentiation is accomplished during progenitor cell divisions in vivo.
Asymmetric inheritance of the apical domain and self-renewal of retinal ganglion cell progenitors depend on Anillin function
These authors contributed equally to this work
Currently Viewing Accepted Manuscript - Newer Version Available
Alessio Paolini, Anne-Laure Duchemin, Shahad Albadri, Eva Patzel, Dorothee Bornhorst, Paula González Avalos, Steffen Lemke, Anja Machate, Michael Brand, Saadettin Sel, Vincenzo Di Donato, Filippo Del Bene, Flavio R. Zolessi, Mirana Ramialison, Lucia Poggi; Asymmetric inheritance of the apical domain and self-renewal of retinal ganglion cell progenitors depend on Anillin function. Development 2015; dev.118612. doi: https://doi.org/10.1242/dev.118612
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