Algorithmic profiling as a source of hermeneutical injustice.

It is well-established that algorithms can be instruments of injustice. It is less frequently discussed, however, how current modes of AI deployment often make the very discovery of injustice difficult, if not impossible. In this article, we focus on the effects of algorithmic profiling on epistemic agency.

The role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis.

Processing bodies (P-bodies) are cytoplasmic membrane-less organelles which host multiple mRNA processing events. While the fundamental principles of P-body organization are beginning to be elucidated in vitro, a nuanced understanding of how their assembly is regulated in vivo remains elusive. Here, we investigate the potential link between ER exit sites and P-bodies in Drosophila melanogaster egg chambers.

Post-transcriptional regulation of and mRNAs is mediated by Bruno 1 and Cup, and further fine-tuned within P-bodies.

Cell cycle progression is tightly controlled by the regulated synthesis and degradation of Cyclins, such as Cyclin A and Cyclin B, which activate CDK1 to trigger mitosis. Mutations affecting Cyclin regulation are often linked to tumorigenesis, making the study of cyclin mRNA regulation critical for identifying new cancer therapies. In this study, we demonstrate via super-resolution microscopy that and mRNAs associate with Bruno 1 and Cup in nurse cells.

The mRNA dynamics underpinning translational control mechanisms of Drosophila melanogaster oogenesis.

Advances in the study of mRNAs have yielded major new insights into post-transcriptional control of gene expression. Focus on the spatial regulation of mRNAs in highly polarized cells has demonstrated that mRNAs translocate through cells as mRNA:protein granules (mRNPs). These complex self-assemblies containing nuclear and cytoplasmic proteins are fundamental to the coordinated translation throughout cellular development.

Distinct conformational states enable transglutaminase 2 to promote cancer cell survival versus cell death.

Transglutaminase 2 (TG2) is a GTP-binding, protein-crosslinking enzyme that has been investigated as a therapeutic target for Celiac disease, neurological disorders, and aggressive cancers. TG2 has been suggested to adopt two conformational states that regulate its functions: a GTP-bound, closed conformation, and a calcium-bound, crosslinking-active open conformation. TG2 mutants that constitutively adopt an open conformation are cytotoxic to cancer cells.