Publications by authors named "M Esther Farez-Vidal"

Plakophilin 1 (PKP1), a member of the p120ctn subfamily of the armadillo (ARM)-repeat-containing proteins, is an important structural component of cell-cell adhesion scaffolds although it can also be ubiquitously found in the cytoplasm and the nucleus. RYBP (RING 1A and YY1 binding protein) is a multifunctional intrinsically disordered protein (IDP) best described as a transcriptional regulator. Both proteins are involved in the development and metastasis of several types of tumors.

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Microbes live within complex communities of interacting populations, either free-living in waters and soils or symbionts of animals and plants. Their interactions include the production of antimicrobial peptides (bacteriocins) to antagonize competitors, and these producers must carry their own immunity gene for self-protection. Whether other coexisting populations are sensitive or resistant to the bacteriocin producer will be key for the population dynamics within the microbial community.

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Article Synopsis
  • Plakophilin 1 (PKP1) is a structural protein involved in cell adhesion and found in various cellular locations, while PADI4 is an enzyme associated with converting arginine to citrulline and is present in immune cells and cancer cells.
  • The binding between PKP1 and PADI4 was investigated using various biophysical techniques, revealing a strong interaction with a dissociation constant around 1 μM, which was confirmed by multiple methods, including Western blotting.
  • This research is significant as it offers new insights into the relationship between these proteins, potentially contributing to our understanding of tumor development and the formation of neutrophil extracellular traps (NETs), which impact cell adhesion.
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Purpose: Plakophilin 1 (PKP1) is well-known as an important component of the desmosome, a cell structure specialized in spot-like cell-to-cell adhesion. Although desmosomes have generally been associated with tumor suppressor functions, we recently found that PKP1 is recurrently overexpressed in squamous cell lung cancer (SqCLC) to exert an oncogenic role by enhancing the translation of MYC (c-Myc), a major oncogene. In this study, we aim to further characterize the functional relationship between PKP1 and MYC.

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In their struggle for life, bacteria frequently produce antagonistic substances against competitors. Antimicrobial peptides produced by bacteria (known as bacteriocins) are active against other bacteria, but harmless to their producer due to an associated immunity gene that prevents self-inhibition. However, knowledge of cross-resistance between different types of bacteriocin producer remains very limited.

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