Ihem

The scaffold protein 14-3-3ζ is an established regulator of adipogenesis and postnatal adiposity. We and others have demonstrated that the 14-3-3ζ interactome to be diverse and dynamic, and it can be examined to identify novel regulators of physiological processes, including adipogenesis. In the present study, we sought to determine if factors that influence adipogenesis could be identified in the 14-3-3ζ interactome found in white adipose tissue of lean or obese TAP-tagged-14-3-3ζ overexpressing mice. Using mass spectrometry, changes in the abundance of novel, as well as established, adipogenic factors within the 14-3-3ζ interactome could detected. One novel candidate is plakoglobin, the homolog of the known adipogenic inhibitor β-catenin, and herein, we report that plakoglobin is involved in adipocyte differentiation. Plakoglobin is expressed in murine 3T3-L1 cells and is primarily localized to the nucleus, where its abundance decreases during adipogenesis. Ectopic overexpression ...

In this study, we propose an automatic procedure for digital image processing. We describe a method that can efficiently quantify and characterize lipid droplets distributions in different cell types in culture. Prospectively, the lipid droplets detection method described in this work could be applied to static or time-lapse data, collected with a simple visible light or fluorescence microscopy equipment. Fully automated algorithms were implemented in Octave, a freely available scientific package.

The SARS-CoV-2 N protein binds several cell host proteins including 14-3-3g, a well-characterized regulatory protein. However, the biological function of this interaction is not completely understood. We analyzed the variability of~90 000 sequences of the SARS-CoV-2 N protein, particularly, its mutations in disordered regions containing binding motifs for 14-3-3 proteins. We studied how these mutations affect the binding energy to 14-3-3g and found that changes positively affecting the predicted interaction with 14-3-3g are the most successfully spread, with the highest prevalence in the phylogenetic tree. Although most residues are highly conserved within the 14-3-3 binding site, compensatory mutations to maintain the interaction energy of N-14-3-3g were found, including half of the current variants of concern and interest. Our results suggest that binding of N to 14-3-3g is beneficial for the virus, thus targeting this viral-host protein-protein interaction seems an attractive approach to explore antiviral strategies.

The scaffold protein 14-3-3ζ is an established regulator of adipogenesis and postnatal adiposity. We and others have demonstrated that the 14-3-3ζ interactome to be diverse and dynamic, and it can be examined to identify novel regulators of physiological processes, including adipogenesis. In the present study, we sought to determine if factors that influence adipogenesis could be identified in the 14-3-3ζ interactome found in white adipose tissue of lean or obese TAP-tagged-14-3-3ζ overexpressing mice. Using mass spectrometry, changes in the abundance of novel, as well as established, adipogenic factors within the 14-3-3ζ interactome could detected. One novel candidate is plakoglobin, the homolog of the known adipogenic inhibitor β-catenin, and herein, we report that plakoglobin is involved in adipocyte differentiation. Plakoglobin is expressed in murine 3T3-L1 cells and is primarily localized to the nucleus, where its abundance decreases during adipogenesis. Ectopic overexpression and siRNA-mediated depletion of plakoglobin had dual effects on inhibiting adipogenesis and reducing PPARγ2 expression. Plakoglobin depletion in human adipose-derived stem cells also impaired adipogenesis and reduced lipid accumulation post-differentiation. Transcriptional assays indicated that plakoglobin does not participate in Wnt/β-catenin signaling, as its depletion did not affect Wnt3a-mediated SUPERTOPFlash activity. Taken together, our results establish plakoglobin as a novel regulator of adipogenesis in vitro and highlights the ability of using the 14-3-3ζ interactome to discover undiscovered pro-obesogenic factors. .

The SARS-CoV-2 N protein binds several cell host proteins including 14-3-3g, a well-characterized regulatory protein. However, the biological function of this interaction is not completely understood. We analyzed the variability of~90 000 sequences of the SARS-CoV-2 N protein, particularly, its mutations in disordered regions containing binding motifs for 14-3-3 proteins. We studied how these mutations affect the binding energy to 14-3-3g and found that changes positively affecting the predicted interaction with 14-3-3g are the most successfully spread, with the highest prevalence in the phylogenetic tree. Although most residues are highly conserved within the 14-3-3 binding site, compensatory mutations to maintain the interaction energy of N-14-3-3g were found, including half of the current variants of concern and interest. Our results suggest that binding of N to 14-3-3g is beneficial for the virus, thus targeting this viral-host protein-protein interaction seems an attractive approach to explore antiviral strategies.

In this work, the formation of capsules in xanthan gum and complexing solutions of Fe III is structurally evaluated. These capsules have a spheroid shape that, when dried, collapse into disc shapes. These spheroids are made up of microspheres that partially explain this collapse. The backscattered SEM image shows areas rich in Fe and others poorer in this metal, the EDX analysis confirms this. FTIR chromatograms show a clear shift at approximately 1620 cm-1 due to the formation of the xanthan gum-Fe III complex. This work also proposes a structure, theoretically demonstrated, between xanthan gum and Fe III, which can explain what the biopolymeric structure bending procedure is like due to the presence of Fe III, a model called TransbiHook.