Publications by authors named "Marc Balan"
Article Synopsis
- The PAR-1-MARK pathway regulates cell polarity by phosphorylating microtubule-associated proteins, specifically ARHGEF2.
- Liver kinase B1 (LKB1) activates MARK3, leading to the phosphorylation of ARHGEF2, which disrupts its binding to DYNLT1 and promotes RHOA activation.
- This phosphorylation is crucial for forming stress fibers and maintaining organized cellular structures, highlighting a regulatory mechanism that connects microtubules and the actin cytoskeleton in epithelial cells.
For almost 40 years, it has been known that tryptophan metabolites and picolinic acid analogues act as inhibitors of gluconeogenesis. Early studies observed that 3-mercaptopicolinic acid (MPA) was a potent hypoglycemic agent via inhibition of glucose synthesis through the specific inhibition of phosphoenolpyruvate carboxykinase (PEPCK) in the gluconeogenesis pathway. Despite prior kinetic investigation, the mechanism of the inhibition by MPA is unclear.
View Article and Find Full Text PDFActin-based stress fiber formation is coupled to microtubule depolymerization through the local activation of RhoA. While the RhoGEF Lfc has been implicated in this cytoskeleton coupling process, it has remained elusive how Lfc is recruited to microtubules and how microtubule recruitment moderates Lfc activity. Here, we demonstrate that the dynein light chain protein Tctex-1 is required for localization of Lfc to microtubules.
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