Publications by authors named "Mabel Jouve San Roman"

Cells secrete extracellular vesicles (EVs) and non-vesicular extracellular (nano)particles (NVEPs or ENPs) that may play a role in intercellular communication. Tumor-derived EVs have been proposed to induce immune priming of antigen presenting cells or to be immuno-suppressive agents. We suspect that such disparate functions are due to variable compositions in EV subtypes and ENPs.

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The positive effects of therapeutic human allogeneic cardiac stem/progenitor cells (hCPC) in terms of cardiac repair/regeneration are very likely mediated by paracrine effects. Our previous studies revealed the advantageous immune interactions of allogeneic hCPC and proposed them as part of the positive paracrine effects occurring upon their application postmyocardial infarction (MI). Currently, extracellular vesicles/exosomes (EV/Exs) released by stem/progenitor cells are also proposed as major mediators of paracrine effects of therapeutic cells.

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Proteins of the Bin/amphiphysin/Rvs (BAR) domain superfamily are essential in controlling the shape and dynamics of intracellular membranes. Here, we present evidence for the unconventional function of a member of the endophilin family of BAR and Src homology 3 domain-containing proteins, namely endophilin B2, in the perinuclear organization of intermediate filaments. Using mass spectrometry analysis based on capturing endophilin B2 partners in in situ pre-established complexes in cells, we unravel the interaction of endophilin B2 with plectin 1, a variant of the cytoskeleton linker protein plectin as well as with vimentin.

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Article Synopsis
  • BAR domain-containing proteins, like endophilins, play a critical role in controlling membrane dynamics and processes such as endocytosis and autophagy due to their unique crescent-shaped structures.
  • The study identifies that a specific part of the endophilin A protein, particularly the third α-helix and the leucine 215 residue, is crucial for the dimerization process, impacting how these proteins interact with membranes and other protein partners.
  • Substituting leucine 215 with aspartate significantly alters the protein's membrane binding and shaping abilities, indicating that even small changes in protein structure can affect cell functionalities, such as the recycling of transferrin receptors.
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