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| http://dx.doi.org/10.1091/mbc.E15-01-0022 | DOI Listing |
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SNARE-Mediated Membrane Fusion Probed Using a Synthetic Organelle in the Living Bacterium.
Methods Mol Biol
January 2025
Université Paris Cité, Institute of Psychiatry and Neuroscience of Paris (IPNP), INSERM U1266, Paris, France.
Studies on the mechanisms and regulation of functional assemblies of SNARE proteins mediating membrane fusion essentially make use of recombinant proteins and artificial phospholipid bilayers. We have developed an easy-to-use in vivo system reconstituting membrane fusion in living bacteria. It relies on the formation of caveolin-dependent intracytoplasmic cisternae followed by the controlled synthesis of members of the synaptic SNARE machinery.
View Article and Find Full Text PDF3D-Porous Electrocatalyst with Tip-Enhanced Electric Field Effect Enables High-Performance Proton Exchange Membrane Water Electrolyzer.
Adv Mater
January 2025
School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu, 210023, China.
Hydrogen evolution reaction (HER), as one of the most advanced methods for the green production of hydrogen, is greatly impeded by inefficient mass transfer. Here we present an efficiently reactant enriched and mass traffic system by integrating high-curvature Pt nanocones with 3D porous TiAl framework to enhance mass transfer rate. Theoretical simulations, in situ Raman spectroscopy and potential-dependent Fourier transform infrared spectroscopy results disclose that the strong local electric field induced by high-curvature Pt can greatly promote the HO supply rate during HER, resulting in ∼1.
View Article and Find Full Text PDFThe conserved K3 residue in the N-terminal region of Rab10 small GTPase is required for tubular endosome formation: N-terminal tagging causes Rab10 dysfunction.
J Cell Sci
January 2025
Laboratory of Membrane Trafficking Mechanisms, Department of Integrative Life Sciences, Graduate School of Life Sciences, Tohoku University, Aobayama, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
Various N-terminal tags have often been used to identify the functions and localization of Rab small GTPases, but their impact on Rab proteins themselves has been poorly investigated. Here, we used a knockout (KO)-rescue approach to systematically evaluate the effect of N-terminal tagging of two Rabs, Rab10 and Rab27A, on Rab10-KO HeLa cells and Rab27A-deficient melanocytes (melan-ash cells), respectively. The results showed that all of the N-terminal-tagged Rab27A proteins mediated actin-based melanosome transport in the melan-ash cells, but none of the N-terminal-tagged Rab10 proteins fully rescued the defect in tubular endosome formation in the Rab10-KO cells.
View Article and Find Full Text PDFApolipoprotein-L Functions in Membrane Remodeling.
Cells
December 2024
Laboratory of Molecular Parasitology, Institut de Biologie et de Médecine Moléculaires (IBMM), Université Libre de Bruxelles, 6041 Gosselies, Belgium.
The mammalian Apolipoprotein-L families (APOLs) contain several isoforms of membrane-interacting proteins, some of which are involved in the control of membrane dynamics (traffic, fission and fusion). Specifically, human APOL1 and APOL3 appear to control membrane remodeling linked to pathogen infection. Through its association with Non-Muscular Myosin-2A (NM2A), APOL1 controls Golgi-derived trafficking of vesicles carrying the lipid scramblase Autophagy-9A (ATG9A).
View Article and Find Full Text PDFUnlabelled: Endocytic recycling of transmembrane proteins is essential to cell signaling, ligand uptake, protein traffic and degradation. The intracellular domains of many transmembrane proteins are ubiquitylated, which promotes their internalization by clathrin-mediated endocytosis. How might this enhanced internalization impact endocytic uptake of transmembrane proteins that lack ubiquitylation? Recent work demonstrates that diverse transmembrane proteins compete for space within highly crowded endocytic structures, suggesting that enhanced internalization of one group of transmembrane proteins may come at the expense of other groups.
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