Articles by Elena Rebollo in JoVE
AFM and Microrheology in the Zebrafish Embryo Yolk Cell Maria Marsal1, Ignasi Jorba2, Elena Rebollo1, Tomas Luque2, Daniel Navajas2, Enrique Martín-Blanco1 1Instituto de Biología Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, 2Institute for Bioengineering of Catalonia, Universitat de Barcelona and CIBER Enfermedades Respiratorias The lack of tools to measure material properties and tensional parameters in vivo prevents validating their roles during development. We employed atomic force microscopy (AFM) and nanoparticle-tracking to quantify mechanical features on the intact zebrafish embryo yolk cell during epiboly. These methods are reliable and widely applicable avoiding intrusive interventions.
Other articles by Elena Rebollo on PubMed
Live Imaging in Drosophila: The Optical and Genetic Toolkits Methods (San Diego, Calif.). | Pubmed ID: 24814031 Biological imaging based on light microscopy comes at the core of the methods that let us understanding morphology and its dynamics in synergy to the spatiotemporal distribution of cellular and molecular activities as the organism develops and becomes functional. Non-linear optical tools and superesolution methodologies are under constant development and their applications to live imaging of whole organisms keep improving as we speak. Genetically coded biosensors, multicolor clonal methods and optogenetics in different organisms and, in particular, in Drosophila follow equivalent paths. We anticipate a brilliant future for live imaging providing the roots for the holistic understanding, rather than for individual parts, of development and function at the whole-organism level.
Cold Temperature Induces the Reprogramming of Proteolytic Pathways in Yeast The Journal of Biological Chemistry. | Pubmed ID: 26601941 Despite much evidence of the involvement of the proteasome-ubiquitin signaling system in temperature stress response, the dynamics of the ubiquitylome during cold response has not yet been studied. Here, we have compared quantitative ubiquitylomes from a strain deficient in proteasome substrate recruitment and a reference strain during cold response. We have observed that a large group of proteins showing increased ubiquitylation in the proteasome mutant at low temperature is comprised by reverses suppressor of Ty-phenotype 5 (Rsp5)-regulated plasma membrane proteins. Analysis of internalization and degradation of plasma membrane proteins at low temperature showed that the proteasome becomes determinant for this process, whereas, at 30 °C, the proteasome is dispensable. Moreover, our observations indicate that proteasomes have increased capacity to interact with lysine 63-polyubiquitylated proteins during low temperature in vivo. These unanticipated observations indicate that, during cold response, there is a proteolytic cellular reprogramming in which the proteasome acquires a role in the endocytic-vacuolar pathway.