Research Topics
| N BorgeseSummaryAffiliation: University of Milan Country: Italy Publications
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Detail Information
Publications
Trafficking of tail-anchored proteins: transport from the endoplasmic reticulum to the plasma membrane and sorting between surface domains in polarised epithelial cellsAlessandra Bulbarelli
Consiglio Nazionale delle Ricerche Cellular and Molecular Pharmacology Center and Department of Medical Pharmacology, University of Milan, Milan, Italy
J Cell Sci 115:1689-702. 2002..The two GFP fusion proteins showed a different surface distribution, which is consistent with a role for the two syntaxin TMDs in polarised sorting...
KDEL and KKXX retrieval signals appended to the same reporter protein determine different trafficking between endoplasmic reticulum, intermediate compartment, and Golgi complexMariano Stornaiuolo
Department of Biochemistry and Medical Biotechnology, University of Naples Federico II, Italy
Mol Biol Cell 14:889-902. 2003..These results illustrate how different retrieval signals determine different trafficking patterns and pose novel questions on the underlying molecular mechanisms...- The tale of tail-anchored proteins: coming from the cytosol and looking for a membraneNica Borgese
Consiglio Nazionale delle Ricerche Institute for Neuroscience, Cellular and Molecular Pharmacology Section, Via Vanvitelli 32, 20129 Milano, Italy
J Cell Biol 161:1013-9. 2003.... - Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid compositionSilvia Brambillasca
CNR Institute of Neuroscience - Cell Mol Pharmacology - and Department of Medical Pharmacology, University of Milan, Milan, Italy
EMBO J 24:2533-42. 2005..These results identify the minimal requirements for transmembrane topogenesis of a TA protein and suggest that selectivity among various intracellular compartments can be imparted by differences in their lipid composition... - How tails guide tail-anchored proteins to their destinationsNica Borgese
National Research Council Institute for Neuroscience and Department of Medical Pharmacology, University of Milan, Via Vanvitelli 32, 20129 Milano, Italy
Curr Opin Cell Biol 19:368-75. 2007..Unravelling these pathways will shed light on the biosynthesis and regulation of an important group of membrane proteins and is likely to lead to new concepts in the field of membrane biogenesis... 
Targeting pathways of C-tail-anchored proteinsNica Borgese
National Research Council Institute for Neuroscience and Department of Medical Pharmacology, University of Milan, Milano, Italy
Biochim Biophys Acta 1808:937-46. 2011..This article is part of a Special Issue entitled Protein translocation across or insertion into membranes...- Biogenesis of tail-anchored proteinsN Borgese
Consiglio Nazionale delle Ricerche Institute for Neuroscience, Cellular and Molecular Pharmacology Section, University of Milan, Via Vanvitelli 32, 20129 Milan, Italy
Biochem Soc Trans 31:1238-42. 2003..Here we summarize recent results on the insertion of tail-anchored proteins and discuss possible mechanisms that could be involved... - Remote origins of tail-anchored proteinsNica Borgese
Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Pharmacology, Universita degli Studi di Milano, Via Vanvitelli 32, 20129 Milano, Italy
Traffic 11:877-85. 2010..Thus, eukaryotes may have inherited the GET3 targeting pathway from our archeal ancestor, while the bacterial homologue may be exclusively dedicated to heavy metal resistance... - Endoplasmic reticulum architecture: structures in fluxNica Borgese
National Research Council Institute for Neuroscience and Department of Medical Pharmacology, University of Milan, Via Vanvitelli 32, 20129 Milano, Italy
Curr Opin Cell Biol 18:358-64. 2006..The mechanisms that modulate ER structure are likely to be important for the generation of the characteristic shapes of other organelles... - Targeting of a tail-anchored protein to endoplasmic reticulum and mitochondrial outer membrane by independent but competing pathwaysN Borgese
Consiglio Nazionale delle Ricerche, Cellular and Molecular Pharmacology Center and Department of Medical Pharmacology, University of Milan, Milan, Italy
Mol Biol Cell 12:2482-96. 2001..Thus, targeting occurs directly from the cytosol. Moreover, ER and MOM compete for the same polypeptide, explaining the dual localization of some TA proteins... - A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranesN Borgese
Consiglio Nazionale delle Ricerche Cellular and Molecular Pharmacology Center, Department of Pharmacology, University of Milan, Italy
J Cell Biol 135:1501-13. 1996..Our results indicate that myristoylated reductase localizes to ER and mitochondria by different mechanisms, and reveal a novel role for myristic acid in protein targeting... - An erythroid-specific transcript generates the soluble form of NADH-cytochrome b5 reductase in humansA Bulbarelli
Consiglio Nazionale delle Ricerche Center for Cellular and Molecular Pharmacology, Department of Pharmacology, University of Milan, Milan, Italy
Blood 92:310-9. 1998..Our results indicate that the S-transcript is expressed at late stages of erythroid maturation to generate soluble b5R... - Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulumPaolo Ronchi
Consiglio Nazionale delle Ricerche, Institute of Neuroscience, Cellular and Molecular Pharmacology, University of Milan, 20129 Milan, Italy
J Cell Biol 181:105-18. 2008..Thus, physicochemical features of the TMD influence sorting of membrane proteins both within the ER and at the ER-Golgi boundary by simple receptor-independent mechanisms based on partitioning... - The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl-terminal regionM De Silvestris
C N R Center for Cytopharmacology, Milano, Italy
FEBS Lett 370:69-74. 1995..The chimera localized to mitochondria, indicating that the carboxyl-terminal 43 amino acids of OM b5 contain sufficient information to target the catalytic domain of ER b5 to the mitochondrial outer membrane... - Dynamic and reversible restructuring of the ER induced by PDMP in cultured cellsTeresa Sprocati
Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Medical Pharmacology, Via Vanvitelli 32, University of Milano, 20129 Milano, Italy
J Cell Sci 119:3249-60. 2006..Our results demonstrate a dynamic relationship between smooth and rough ER and have implications for the mechanisms regulating ER architecture... - Unassisted translocation of large polypeptide domains across phospholipid bilayersSilvia Brambillasca
Cellular and Molecular Pharmacology Section, Consiglio Nazionale delle Ricerche Institute of Neuroscience, University of Milan, 20129 Milan, Italy
J Cell Biol 175:767-77. 2006..Our data resolve long-standing discrepancies on TA protein insertion and are relevant to membrane evolution, biogenesis, and physiology... - The role of cytosolic proteins in the insertion of tail-anchored proteins into phospholipid bilayersSara F Colombo
CNR Institute for Neuroscience and Department of Pharmacology, Universita degli Studi di Milano, Italy
J Cell Sci 122:2383-92. 2009..The effect of diamide is also observed in living cells. Thus, the specific in vivo targeting of b5 might be achieved by interaction with redox-sensitive targeting factors that hinder its nonspecific insertion into any permissive bilayer... - N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioningSara Colombo
Consiglio Nazionale delle Ricerche Institute of Neuroscience, Cellular and Molecular Pharmacology Section and Department of Medical Pharmacology, University of Milan, 20129 Milan, Italy
J Cell Biol 168:735-45. 2005..Thus, competition between two cotranslational events, binding of signal recognition particle and modification by N-myristoylation, determines the site of translation and the localization of b5R... - A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulumElisa Fasana
Consiglio Nazionale delle Ricerche Institute of Neuroscience, Via Vanvitelli 32, 20129 Milano, Italy
FASEB J 24:1419-30. 2010..Our results demonstrate that the ALS-linked VAPB mutant causes dramatic ER restructuring that may underlie its pathogenicity in motoneurons... - Translocation of the C terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocationMonica Yabal
Program of Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, Viikinkaari 9, 00710 Helsinki, Finland
J Biol Chem 278:3489-96. 2003..Thus, translocation of tail-anchored b(5)-Nglyc proceeds by a mechanism different from that of signal peptide-driven post-translational translocation... - Formation of stacked ER cisternae by low affinity protein interactionsErik L Snapp
Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, 18 Library Dr, Bldg 18T, Rm 101, Bethesda, MD 20892, USA
J Cell Biol 163:257-69. 2003..This mechanism may underlie the formation of other stacked membrane structures within cells... - Endothelial nitric oxide synthase is segregated from caveolin-1 and localizes to the leading edge of migrating cellsStefania Bulotta
Department of Pharmaco-Biological Science, University of Catanzaro Magna Graecia, 88021 Catanzaro, Italy
Exp Cell Res 312:877-89. 2006..Our results provide a morphological correlate for the role of eNOS in cell migration and raise questions on the site of interaction between eNOS and caveolin-1... - Two tail-anchored protein variants, differing in transmembrane domain length and intracellular sorting, interact differently with lipidsPaolo Ceppi
Department of Experimental, Environmental Medicine, and Biotechnologies (DIMESAB, Medical School, University of Milano-Bicocca, 20052 Monza, Italy
Proc Natl Acad Sci U S A 102:16269-74. 2005..The dissimilar interaction with lipids of these two differently localized TA proteins could have implications for their intracellular sorting...