Coordinated Formation of IMPDH2 Cytoophidium in Mouse Oocytes and Granulosa Cells.

Inosine monophosphate dehydrogenase (IMPDH), the rate-limiting enzyme catalyzing biosynthesis of guanine nucleotides, aggregates under certain circumstances into a type of non-membranous filamentous macrostructure termed "cytoophidium" or "rod and ring" in several types of cells. However, the biological significance and underlying mechanism of IMPDH assembling into cytoophidium remain elusive. In mouse ovaries, IMPDH is reported to be crucial for the maintenance of oocyte-follicle developmental synchrony by providing GTP substrate for granulosa cell natriuretic peptide C/natriuretic peptide receptor 2 (NPPC/NPR2) system to produce cGMP for sustaining oocyte meiotic arrest.

DPAGT1-Mediated Protein -Glycosylation Is Indispensable for Oocyte and Follicle Development in Mice.

Post-translational modification of proteins by -linked glycosylation is crucial for many life processes. However, the exact contribution of -glycosylation to mammalian female reproduction remains largely undefined. Here, DPAGT1, the enzyme that catalyzes the first step of protein -glycosylation, is identified to be indispensable for oocyte development in mice.