Publications by authors named "Javier Hervas"

ATG9A and ATG2A are essential core members of the autophagy machinery. ATG9A is a lipid scramblase that allows equilibration of lipids across a membrane bilayer, whereas ATG2A facilitates lipid flow between tethered membranes. Although both have been functionally linked during the formation of autophagosomes, the molecular details and consequences of their interaction remain unclear.

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Externalization of the phospholipid cardiolipin (CL) to the outer mitochondrial membrane has been proposed to act as a mitophagy trigger. CL would act as a signal for binding the LC3 macroautophagy/autophagy proteins. As yet, the behavior of the LC3-subfamily members has not been directly compared in a detailed way.

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Traditionally, earthquake impact assessments have been made via fieldwork by non-governmental organisations (NGO's) sponsored data collection; however, this approach is time-consuming, expensive and often limited. Recently, social media (SM) has become a valuable tool for quickly collecting large amounts of first-hand data after a disaster and shows great potential for decision-making. Nevertheless, extracting meaningful information from SM is an ongoing area of research.

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Article Synopsis
  • In 2008, guidelines were established for researching autophagy, which has since gained significant interest and new technologies, necessitating regular updates to monitoring methods across various organisms.
  • The new guidelines emphasize selecting appropriate techniques to evaluate autophagy while noting that no single method suits all situations; thus, a combination of methods is encouraged.
  • The document highlights that key proteins involved in autophagy also impact other cellular processes, suggesting genetic studies should focus on multiple autophagy-related genes to fully understand these pathways.
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Autophagy is traditionally depicted as a signaling cascade that culminates in the formation of an autophagosome that degrades cellular cargo. However, recent studies have identified myriad pathways and cellular organelles underlying the autophagy process, be it as signaling platforms or through the contribution of proteins and lipids. The Golgi complex is recognized as being a central transport hub in the cell, with a critical role in endocytic trafficking and endoplasmic reticulum (ER) to plasma membrane (PM) transport.

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Autophagy is an important cellular process in which cell components are degraded in a controlled way and their building blocks are recycled into new macromolecules. Autophagy starts within a double-membrane container, the autophagosome, itself the result of a number of interconversions of cell membranous elements. In our recent work, we have described reconstituted model systems for the interactions of autophagy proteins with membrane lipid bilayers and for the autophagy protein-mediated vesicle tethering and fusion, with the aim of ultimately reconstituting the autophagosome formation.

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Specific protein-lipid interactions lead to a gradual recruitment of AuTophaGy-related (ATG) proteins to the nascent membrane during autophagosome (AP) formation. ATG3, a key protein in the movement of LC3 towards the isolation membrane, has been proposed to facilitate LC3/GABARAP lipidation in highly curved membranes. In this work we have performed a biophysical study of human ATG3 interaction with membranes containing phosphatidylethanolamine, phosphatidylcholine and anionic phospholipids.

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The use of Spatial Division Multiplexing for Microwave Photonics signal processing is proposed and experimentally demonstrated, for the first time to our knowledge, based on the selective inscription of Bragg gratings in homogeneous multicore fibers. The fabricated devices behave as sampled true time delay elements for radiofrequency signals offering a wide range of operation possibilities within the same optical fiber. The key to processing flexibility comes from the implementation of novel multi-cavity configurations by inscribing a variety of different fiber Bragg gratings along the different cores of a 7-core fiber.

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The phospholipid cardiolipin (CL) has been proposed to play a role in selective mitochondrial autophagy, or mitophagy. CL externalization to the outer mitochondrial membrane would act as a signal for the human Atg8 ortholog subfamily, MAP1LC3 (LC3). The latter would mediate both mitochondrial recognition and autophagosome formation, ultimately leading to removal of damaged mitochondria.

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This paper presents a Fabry-Perot fiber tip sensor based on an air-liquid filled cavity. The cavity is sealed off by a thin gold coated membrane of parylene C, between 300 and 350 nm, creating a particularly flexible diaphragm. In order to retrieve and track the cavity of interest from other cavities formed within the sensor tip, a signal processing of the feedback signal is performed by inverse fast Fourier transform.

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Autophagy, an important catabolic pathway involved in a broad spectrum of human diseases, implies the formation of double-membrane-bound structures called autophagosomes (AP), which engulf material to be degraded in lytic compartments. How APs form, especially how the membrane expands and eventually closes upon itself, is an area of intense research. Ubiquitin-like ATG8 has been related to both membrane expansion and membrane fusion, but the underlying molecular mechanisms are poorly understood.

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We present new kind of microwave phase shifters (MPS) based on dispersion of PbS colloidal quantum dots (QDs) in commercially available photoresist SU8 after a ligand exchange process. Ridge PbS-SU8 waveguides are implemented by integration of the nanocomposite in a silicon platform. When these waveguides are pumped at wavelengths below the band-gap of the PbS QDs, a phase shift in an optically conveyed (at 1550 nm) microwave signal is produced.

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Human phospholipid scramblase 1 (SCR) consists of a large cytoplasmic domain and a small presumed transmembrane domain near the C-terminal end of the protein. Previous studies with the SCRΔ mutant lacking the C-terminal portion (last 28 aa) revealed the importance of this C-terminal moiety for protein function and calcium-binding affinity. The present contribution is intended to elucidate the effect of the transmembrane domain suppression on SCRΔ binding to model membranes (lipid monolayers and bilayers) and on SCRΔ reconstitution in proteoliposomes.

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