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MitoNEET-dependent formation of intermitochondrial junctions.
Proc Natl Acad Sci U S A
August 2017
Faculty of Medicine, Department of Cell Physiology and Metabolism, University of Geneva, Centre Médical Universitaire, CH1211 Geneva 4, Switzerland;
MitoNEET (mNEET) is a dimeric mitochondrial outer membrane protein implicated in many facets of human pathophysiology, notably diabetes and cancer, but its molecular function remains poorly characterized. In this study, we generated and analyzed mNEET KO cells and found that in these cells the mitochondrial network was disturbed. Analysis of 3D-EM reconstructions and of thin sections revealed that genetic inactivation of mNEET did not affect the size of mitochondria but that the frequency of intermitochondrial junctions was reduced.
View Article and Find Full Text PDFSTIM1L traps and gates Orai1 channels without remodeling the cortical ER.
J Cell Sci
April 2015
Department of Cell Physiology and Metabolism, University of Geneva, 1 Rue Michel-Servet CH-1211, Geneva 4, Switzerland
STIM proteins populate and expand cortical endoplasmic reticulum (ER) sheets to mediate store-operated Ca(2+) entry (SOCE) by trapping and gating Orai channels in ER-plasma membrane clusters. A longer splice variant, STIM1L, forms permanent ER-plasma membrane clusters and mediates rapid Ca(2+) influx in muscle. Here, we used electron microscopy, total internal reflection fluorescence (TIRF) microscopy and Ca(2+) imaging to establish the trafficking and signaling properties of the two STIM1 isoforms in Stim1(-/-)/Stim2(-/-) fibroblasts.
View Article and Find Full Text PDFMitofusin-2 independent juxtaposition of endoplasmic reticulum and mitochondria: an ultrastructural study.
PLoS One
February 2013
Department for Cell Physiology and Metabolism, Centre Médical Universitaire, Geneva Faculty of Medicine, Geneva, Switzerland.
Besides its role in controlling the morphology of mitochondria, mitofusin-2 has been proposed to tether mitochondria to the endoplasmic reticulum (ER), based largely on light microscopic analysis. In this study we have examined by electron microscopy the organization of ER and mitochondria in cells expressing or not mitofusin-2. Contrary to previous studies, we observed that loss of mitofusin-2 increased ER-mitochondria juxtaposition.
View Article and Find Full Text PDFThe [corrected] SEC23-SEC31 [corrected] interface plays critical role for export of procollagen from the endoplasmic reticulum.
J Biol Chem
March 2012
Section of Genetics, Department of Pediatrics, University of California Davis Medical Center, Sacramento, California 95817,. Electronic address:
COPII proteins are essential for exporting most cargo molecules from the endoplasmic reticulum. The membrane-facing surface of the COPII proteins (especially SEC23-SEC24) interacts directly or indirectly with the cargo molecules destined for exit. As we characterized the SEC23A mutations at the SEC31 binding site identified from patients with cranio-lenticulo-sutural dysplasia, we discovered that the SEC23-SEC31 interface can also influence cargo selection.
View Article and Find Full Text PDFTransmembrane domains control exclusion of membrane proteins from clathrin-coated pits.
J Cell Sci
October 2010
Centre Médical Universitaire, Département de Physiologie Cellulaire et Métabolisme, 1, rue Michel Servet, CH1211 Geneva 4, Switzerland.
Efficient sorting of proteins is essential to allow transport between intracellular compartments while maintaining their specific composition. During endocytosis, membrane proteins can be concentrated in endocytic vesicles by specific interactions between their cytoplasmic domains and cytosolic coat proteins. It is, however, unclear whether they can be excluded from transport vesicles and what the determinants for this sorting could be.
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