Microtearding mode study in NSTX using machine learning enhanced reduced model

This article presents a survey of NSTX cases to study the microtearing mode (MTM) stabilities using the newly developed global reduced model for Slab-Like Microtearing modes (SLiM). A trained neutral network version of SLiM enables rapid assessment (0.05s/mode) of MTM with $98\%$ accuracy providing an opportunity for systemic equilibrium reconstructions based on the matching of experimentally observed frequency bands and SLiM prediction across a wide range of parameters. Such a method finds some success in the NSTX discharges, the frequency observed in the experiment matches with what SLiM predicted. Based on the experience with SLiM analysis, a workflow to estimate the potential MTM frequency for a quick assessment based on experimental observation has been established

Cep152 interacts with Plk4 and is required for centriole duplication

Cep152, the orthologue of Drosophila Asterless, is a Plk4 target that functions with Plk4 in centriole assembly

RNP Export by Nuclear Envelope Budding

Nuclear export of mRNAs is thought to occur exclusively through nuclear pore complexes. In this issue of Cell, Speese et al. identify an alternate pathway for mRNA export in muscle cells where ribonucleoprotein complexes involved in forming neuromuscular junctions transit the nuclear envelope by fusing with and budding through the nuclear membrane

Cep152 interacts with Plk4 and is required for centriole duplication.

Centrioles are microtubule-based structures that organize the centrosome and nucleate cilia. Centrioles duplicate once per cell cycle, and duplication requires Plk4, a member of the Polo-like kinase family; however, the mechanism linking Plk4 activity and centriole formation is unknown. In this study, we show in human and frog cells that Plk4 interacts with the centrosome protein Cep152, the orthologue of Drosophila melanogaster Asterless. The interaction requires the N-terminal 217 residues of Cep152 and the crypto Polo-box of Plk4. Cep152 and Plk4 colocalize at the centriole throughout the cell cycle. Overexpression of Cep152 (1-217) mislocalizes Plk4, but both Cep152 and Plk4 are able to localize to the centriole independently of the other. Depletion of Cep152 prevents both normal centriole duplication and Plk4-induced centriole amplification and results in a failure to localize Sas6 to the centriole, an early step in duplication. Cep152 can be phosphorylated by Plk4 in vitro, suggesting that Cep152 acts with Plk4 to initiate centriole formation