Browsing by Subject "RECRUITMENT"

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Now showing items 21-25 of 25
  • Pfisterer, Simon; Gateva, Gergana; Horvath, Peter; Pirhonen, Juho; Salo, Veijo T.; Karhinen, Leena; Varjosalo, Markku; Ryhänen, Samppa J.; Lappalainen, Pekka; Ikonen, Elina (2017)
    Lipid droplets (LDs) are cellular organelles specialized in triacylglycerol (TG) storage undergoing homotypic clustering and fusion. In non-adipocytic cells with numerous LDs this is balanced by poorly understood droplet dissociation mechanisms. We identify non-muscle myosin IIa (NMIIa/MYH-9) and formin-like 1 (FMNL1) in the LD proteome. NMIIa and actin filaments concentrate around LDs, and form transient foci between dissociating LDs. NMIIa depletion results in decreased LD dissociations, enlarged LDs, decreased hydrolysis and increased storage of TGs. FMNL1 is required for actin assembly on LDs in vitro and for NMIIa recruitment to LDs in cells. We propose a novel acto-myosin structure regulating lipid storage: FMNL1-dependent assembly of myosin II-functionalized actin filaments on LDs facilitates their dissociation, thereby affecting LD surface-to-volume ratio and enzyme accessibility to TGs. In neutrophilic leucocytes from MYH9-related disease patients NMIIa inclusions are accompanied by increased lipid storage in droplets, suggesting that NMIIa dysfunction may contribute to lipid imbalance in man.
  • Fedriani, Jose M.; Garrote, Pedro Jose; Delgado, Maria del Mar; Penteriani, Vincenzo (2015)
    Inland vertebrate predators could enrich of nutrients the local top soils in the area surrounding their nests and dens by depositing faeces, urine, and prey remains and, thus, alter the dynamics of plant populations. Surprisingly, and in contrast with convincing evidence from coastal habitats, whether and how this phenomenon occurs in inland habitats is largely uncertain even though these habitats represent a major fraction of the earth's surface. We investigated during two consecutive breeding seasons the potential enrichment of the top-soils associated with inland ground-nesting eagle owls Bubo bubo, as well as its possible consequences in the growth of two common annual grasses in southern Spain. Top-soils associated with owl nests differed strongly and significantly from control top-soils in chemical parameters, mainly fertility-related properties. Specifically, levels of available phosphorus, total nitrogen, organic matter, and available potassium were 49.1, 5.6, 3.1, and 2.7 times higher, respectively, in top-soils associated with owl nests as compared to control top-soils. Germination experiments in chambers indicated that nutrient enrichment by nesting owls enhanced seedling growth in both annual grasses (Phalaris canariensis and Avena sativa), with seedling size being 1.4-1.3 times higher in owl nest top-soils than in control top-soils. Our experimental study revealed that pervasive inland, predatory birds can profoundly enrich the topsoil around their nests and, thus, potentially enhance local vegetation growth. Because diverse inland vertebrate predators are widespread in most habitats they have a strong potential to enhance spatial heterogeneity, impinge on plant communities, and exert an overlooked effect on primary productivity worldwide.
  • Rahikainen, Rolle; Öhman, Tiina; Turkki, Paula; Varjosalo, Markku; Hytönen, Vesa P. (2019)
    Talin protein is one of the key components in integrin-mediated adhesion complexes. Talins transmit mechanical forces between beta-integrin and actin, and regulate adhesion complex composition and signaling through the force-regulated unfolding of talin rod domain. Using modified talin proteins, we demonstrate that these functions contribute to different cellular processes and can be dissected. The transmission of mechanical forces regulates adhesion complex composition and phosphotyrosine signaling even in the absence of the mechanically regulated talin rod subdomains. However, the presence of the rod subdomains and their mechanical activation are required for the reinforcement of the adhesion complex, cell polarization and migration. Talin rod domain unfolding was also found to be essential for the generation of cellular signaling anisotropy, since both insufficient and excess activity of the rod domain severely inhibited cell polarization. Utilizing proteomics tools, we identified adhesome components that are recruited and activated either in a talin rod-dependent manner or independently of the rod subdomains. This study clarifies the division of roles between the force-regulated unfolding of a talin protein (talin 1) and its function as a physical linker between integrins and the cytoskeleton.
  • Scaramuzzo, Gaetano; Broche, Ludovic; Pellegrini, Mariangela; Porra, Liisa; Derosa, Savino; Tannoia, Angela Principia; Marzullo, Andrea; Borges, Joao Batista; Bayat, Sam; Bravin, Alberto; Larsson, Anders; Perchiazzi, Gaetano (2019)
    Modern ventilatory strategies are based on the assumption that lung terminal airspaces act as isotropic balloons that progressively accommodate gas. Phase contrast synchrotron radiation computed tomography (PCSRCT) has recently challenged this concept, showing that in healthy lungs, deflation mechanisms are based on the sequential de-recruitment of airspaces. Using PCSRCT scans in an animal model of acute respiratory distress syndrome (ARDS), this study examined whether the numerosity (ASnum) and dimension (ASdim) of lung airspaces change during a deflation maneuver at decreasing levels of positive end-expiratory pressure (PEEP) at 12, 9, 6, 3, and 0 cmH(2)O. Deflation was associated with significant reduction of ASdim both in the whole lung section (passing from from 13.1 +/- 2.0 at PEEP 12 to 7.6 +/- 4.2 voxels at PEEP 0) and in single concentric regions of interest (ROIs). However, the regression between applied PEEP and ASnum was significant in the whole slice (ranging from 188 +/- 52 at PEEP 12 to 146.4 +/- 96.7 at PEEP 0) but not in the single ROIs. This mechanism of deflation in which reduction of ASdim is predominant, differs from the one observed in healthy conditions, suggesting that the peculiar alveolar micromechanics of ARDS might play a role in the deflation process.
  • Gateva, Gergana; Kremneva, Elena; Reindl, Theresia; Kotila, Tommi; Kogan, Konstantin; Gressin, Laurene; Gunning, Peter W.; Manstein, Dietmar J.; Michelot, Alphee; Lappalainen, Pekka (2017)
    Actin filaments assemble into a variety of networks to provide force for diverse cellular processes [1]. Tropomyosins are coiled-coil dimers that form head-to-tail polymers along actin filaments and regulate interactions of other proteins, including actin-de polymerizing factor (ADF)/cofilins and myosins, with actin [2-5]. In mammals, >40 tropomyosin isoforms can be generated through alternative splicing from four tropomyosin genes. Different isoforms display non-redundant functions and partially non-overlapping localization patterns, for example within the stress fiber network [6, 7]. Based on cell biological studies, it was thus proposed that tropomyosin isoforms may specify the functional properties of different actin filament populations [2]. To test this hypothesis, we analyzed the properties of actin filaments decorated by stress-fiber-associated tropomyosins (Tpm1.6, Tpm1.7, Tpm2.1, Tpm3.1, Tpm3.2, and Tpm4.2). These proteins bound F-actin with high affinity and competed with a-actinin for actin filament binding. Importantly, total internal reflection fluorescence (TIRF) microscopy of fluorescently tagged proteins revealed that most tropomyosin isoforms cannot co-polymerize with each other on actin filaments. These isoforms also bind actin with different dynamics, which correlate with their effects on actin-binding proteins. The long isoforms Tpm1.6 and Tpm1.7 displayed stable interactions with actin filaments and protected filaments from ADF/cofilin-mediated disassembly, but did not activate non-muscle myosin Ila (NMIIa). In contrast, the short isoforms Tpm3.1, Tpm3.2, and Tpm4.2 displayed rapid dynamics on actin filaments and stimulated the ATPase activity of NMIla, but did not efficiently protect filaments from ADF/cofilin. Together, these data provide experimental evidence that tropomyosin isoforms segregate to different actin filaments and specify functional properties of distinct actin filament populations.