Stable intronic sequence RNAs (sisRNAs) are by-products of splicing and regulate gene expression. How sisRNAs are regulated is unclear. Here we report that a double-stranded RNA binding protein, Disco-interacting protein 1 (DIP1) regulates sisRNAs in Drosophila. DIP1 negatively regulates the abundance of sisR-1 and INE-1 sisRNAs. Fine-tuning of sisR-1 by DIP1 is important to maintain female germline stem cell homeostasis by modulating germline stem cell differentiation and niche adhesion. Drosophila DIP1 localizes to a nuclear body (satellite body) and associates with the fourth chromosome, which contains a very high density of INE-1 transposable element sequences that are processed into sisRNAs. DIP1 presumably acts outside the satellite bodies to regulate sisR-1, which is not on the fourth chromosome. Thus, our study identifies DIP1 as a sisRNA regulatory protein that controls germline stem cell self-renewal in Drosophila.
Spatial control of exocytosis underlies polarized cell morphogenesis. In rod-shaped fission yeast, exocytic vesicles are conveyed along the actin cytoskeleton by myosin V motors toward growing cell ends [1, 2], the major sites for exocytosis. However, actomyosin-based vesicle delivery is dispensable for polarized secretion and cylindrical cell shape of fission yeast [3]. Thus, additional mechanisms should function in the spatial confinement of exocytosis. Here we report a novel role of endoplasmic reticulum (ER)-plasma membrane (PM) contacts in restricting exocytic sites for polarized fission yeast morphogenesis. We show that fission yeast cells deficient in both ER-PM contacts and actomyosin-based secretory vesicle transport display aberrant globular cell shape due to delocalized exocytosis. By artificially manipulating the strength and extent of ER-PM contacts in wild-type and mutant cells that exhibit induced ectopic exocytosis, we demonstrate that exocytosis and ER-PM contact formation are spatially incompatible. Furthermore, extensive ER-PM junctions at the non-growing lateral cell cortex prevent the PM from exocytic vesicle tethering and hence attenuate growth potential at cell sides. We thus propose that ER-PM contacts function as a new morphogenetic module by limiting exocytosis to growing cell tips in fission yeast. A similar mechanism could apply to other cell types with prominent ER-PM contacts.
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