Publications by authors named "Jesica B Flores-Martin"
Background: Arginyltransferase (Ate1) orchestrates posttranslational protein arginylation, a pivotal regulator of cellular proteolytic processes. In eukaryotic cells, two interconnected systems-the ubiquitin proteasome system (UPS) and macroautophagy-mediate proteolysis and cooperate to maintain quality protein control and cellular homeostasis. Previous studies have shown that N-terminal arginylation facilitates protein degradation through the UPS.
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- StarD7 is part of the START protein family, involved in lipid transport and cellular signaling, and its isoforms play different roles in cell function.
- Silencing StarD7 reduces the expression of key proteins (Cx43, integrin β1, and p-ERK1/2) in non-cancerous migrating cells and disrupts their cellular structures.
- Restoring Cx43 levels can regain cell migration abilities, while expressing the StarD7.II isoform enhances migration and the levels of the aforementioned proteins, indicating StarD7's role in cell migration is linked to an ERK1/2/Cx43 pathway.
The ubiquitin-proteasome system (UPS) degrades intracellular proteins through the 26S proteasome. We analysed how cold stress affects the UPS in glial cells. Together with a reduction in the 20S proteolytic activity and increased levels of polyubiquitinated proteins, exposure of glial cell cultures to cold induces a partial disassembly of the 26S proteasome.
View Article and Find Full Text PDFAn increased risk of pregnancy disorders has been reported in women and animal models exposed to organophosphate pesticides. However, less information is available on impacts to human placental function. Here, we addressed the impact of chlorpyrifos (CPF) on extravillous cytotrophoblasts (evCTB) employing HTR8/SVneo cells as an in vitro model.
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