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  • 1
    Publication Date: 2012-03-21
    Description: Transferring lipid antigens from membranes into CD1 antigen-presenting proteins represents a major molecular hurdle necessary for T-cell recognition. Saposins facilitate this process, but the mechanisms used are not well understood. We found that saposin B forms soluble saposin protein–lipid complexes detected by native gel electrophoresis that can directly load CD1 proteins. Because saposin B must bind lipids directly to function, we found it could not accommodate long acyl chain containing lipids. In contrast, saposin C facilitates CD1 lipid loading in a different way. It uses a stable, membrane-associated topology and was capable of loading lipid antigens without forming soluble saposin–lipid antigen complexes. These findings reveal how saposins use different strategies to facilitate transfer of structurally diverse lipid antigens.
    Keywords: Inaugural Articles
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 2
    Publication Date: 2008-07-29
    Description: Ageing and the mortality that ensues are sustainable for the species only if age is reset in newborns. In budding yeast, buds are made young whereas ageing factors, such as carbonylated proteins and DNA circles, remain confined to the ageing mother cell. The mechanisms of this confinement and their relevance are poorly understood. Here we show that a septin-dependent, lateral diffusion barrier forms in the nuclear envelope and limits the translocation of pre-existing nuclear pores into the bud. The retention of DNA circles within the mother cell depends on the presence of the diffusion barrier and on the anchorage of the circles to pores mediated by the nuclear basket. In accordance with the diffusion barrier ensuring the asymmetric segregation of nuclear age-determinants, the barrier mutant bud6Delta fails to properly reset age in buds. Our data involve septin-dependent diffusion barriers in the confinement of ageing factors to one daughter cell during asymmetric cell division.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shcheprova, Zhanna -- Baldi, Sandro -- Frei, Stephanie Buvelot -- Gonnet, Gaston -- Barral, Yves -- England -- Nature. 2008 Aug 7;454(7205):728-34. doi: 10.1038/nature07212. Epub 2008 Jul 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry, Biology Department, ETH Zurich, Schafmattstrasse 18, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18660802" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Cell Aging/*physiology ; *Cell Division ; Cell Polarity/*physiology ; Chromosome Segregation ; Chromosomes, Fungal/genetics/metabolism ; Cytoskeletal Proteins/metabolism ; DNA, Fungal/genetics/metabolism ; Diffusion ; Fluorescence Recovery After Photobleaching ; Microfilament Proteins/metabolism ; Mitosis ; Nuclear Envelope/metabolism ; Plasmids/genetics/metabolism ; Saccharomyces cerevisiae/*cytology/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barral, Yves -- New York, N.Y. -- Science. 2010 Sep 10;329(5997):1289-90. doi: 10.1126/science.1195445.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland. yves.barral@bc.biol.ethz.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829470" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/metabolism/ultrastructure ; *Cell Polarity ; Centrioles/metabolism ; Cilia/*metabolism/ultrastructure ; Cytoskeletal Proteins/chemistry/*metabolism ; Diffusion ; GTP-Binding Proteins/chemistry/*metabolism ; Glycoproteins/genetics/metabolism ; Hedgehog Proteins/metabolism ; Humans ; Mutant Proteins/metabolism ; Mutation ; Receptors, Cell Surface/metabolism ; Signal Transduction ; Xenopus Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2011-03-12
    Description: Partitioning of chromatids during mitosis requires that chromosome compaction and spindle length scale appropriately with each other. However, it is not clear whether chromosome condensation and spindle elongation are linked. Here, we find that yeast cells could cope with a 45% increase in the length of their longest chromosome arm by increasing its condensation. The spindle midzone, aurora/Ipl1 activity, and Ser10 of histone H3 mediated this response. Thus, the anaphase spindle may function as a ruler to adapt the condensation of chromatids, promoting their segregation regardless of chromosome or spindle length.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurohr, Gabriel -- Naegeli, Andreas -- Titos, Iris -- Theler, Dominik -- Greber, Basil -- Diez, Javier -- Gabaldon, Toni -- Mendoza, Manuel -- Barral, Yves -- New York, N.Y. -- Science. 2011 Apr 22;332(6028):465-8. doi: 10.1126/science.1201578. Epub 2011 Mar 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Genomic Regulation (CRG), Barcelona, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21393511" target="_blank"〉PubMed〈/a〉
    Keywords: Aldose-Ketose Isomerases/genetics ; *Anaphase ; Aurora Kinases ; Chromosome Segregation ; Chromosomes, Fungal/genetics/*physiology ; Histones/metabolism ; Intracellular Signaling Peptides and Proteins/genetics/metabolism ; Microtubule-Associated Proteins/genetics/metabolism ; Mutation ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Saccharomyces cerevisiae/genetics/*physiology ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Spindle Apparatus/*physiology/*ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2014-01-05
    Description: Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkins, Bryan J -- Rall, Nils A -- Ostwal, Yogesh -- Kruitwagen, Tom -- Hiragami-Hamada, Kyoko -- Winkler, Marco -- Barral, Yves -- Fischle, Wolfgang -- Neumann, Heinz -- New York, N.Y. -- Science. 2014 Jan 3;343(6166):77-80. doi: 10.1126/science.1244508.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Free Floater (Junior) Research Group "Applied Synthetic Biology," Institute for Microbiology and Genetics, Georg-August University Gottingen, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24385627" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Chromatin/*metabolism ; Chromosomes, Fungal/genetics/metabolism ; Cross-Linking Reagents/chemistry/radiation effects ; DNA-Binding Proteins/metabolism ; Histones/*metabolism ; Lysine/metabolism ; *Mitosis ; Multiprotein Complexes/metabolism ; Phosphorylation ; Protein Interaction Mapping ; *Protein Processing, Post-Translational ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Serine/*metabolism ; Sirtuin 2/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2004-07-17
    Description: During cytokinesis, furrow ingression and plasma membrane fission irreversibly separate daughter cells. How actomyosin ring assembly and contraction, vesicle fusion, and abscission are spatially coordinated was unknown. We found that during cytokinesis septin rings, located on both sides of the actomyosin ring, acted as barriers to compartmentalize the cortex around the cleavage site. Compartmentalization maintained diffusible cortical factors, such as the exocyst and the polarizome, to the site of cleavage. In turn, such factors were required for actomyosin ring function and membrane abscission. Thus, a specialized cortical compartment ensures the spatial coordination of cytokinetic events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dobbelaere, Jeroen -- Barral, Yves -- New York, N.Y. -- Science. 2004 Jul 16;305(5682):393-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry, Swiss Federal Institute of Technology, ETH-Honggerberg, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15256669" target="_blank"〉PubMed〈/a〉
    Keywords: Actomyosin/physiology ; *Cell Compartmentation ; Cell Cycle Proteins/genetics/*metabolism ; *Cell Division ; Chitin Synthase/metabolism ; Cytoskeletal Proteins/genetics/*metabolism ; Green Fluorescent Proteins ; Luminescent Proteins ; Microfilament Proteins/metabolism ; Myosin Heavy Chains/metabolism ; Profilins ; Saccharomyces cerevisiae/*cytology/metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; *ras GTPase-Activating Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2015-09-19
    Description: Throughout life, neural stem cells (NSCs) generate neurons in the mammalian brain. Using photobleaching experiments, we found that during cell division in vitro and within the developing mouse forebrain, NSCs generate a lateral diffusion barrier in the membrane of the endoplasmic reticulum, thereby promoting asymmetric segregation of cellular components. The diffusion barrier weakens with age and in response to impairment of lamin-associated nuclear envelope constituents. Weakening of the diffusion barrier disrupts asymmetric segregation of damaged proteins, a product of aging. Damaged proteins are asymmetrically inherited by the nonstem daughter cell in embryonic and young adult NSC divisions, whereas in the older adult brain, damaged proteins are more symmetrically distributed between progeny. Thus, these data identify a mechanism of how damage that accumulates with age is asymmetrically distributed during somatic stem cell division.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, D L -- Pilz, G A -- Arauzo-Bravo, M J -- Barral, Y -- Jessberger, S -- New York, N.Y. -- Science. 2015 Sep 18;349(6254):1334-8. doi: 10.1126/science.aac9868.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brain Research Institute, Faculty of Medicine and Science, University of Zurich, 8057 Zurich, Switzerland. ; Biodonostia Health Research Institute, 20014 San Sebastian, Spain. IKERBASQUE, Basque Foundation for Science, 48013 Bilbao, Spain. ; Institute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland. ; Brain Research Institute, Faculty of Medicine and Science, University of Zurich, 8057 Zurich, Switzerland. jessberger@hifo.uzh.ch.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26383951" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Aging ; *Cell Division ; Diffusion ; Endoplasmic Reticulum/physiology/ultrastructure ; Intracellular Membranes/physiology/ultrastructure ; Lamin Type A/*metabolism ; Mice ; Neural Stem Cells/*cytology/*metabolism ; Photobleaching ; Prosencephalon/cytology/growth & development/metabolism ; Protein Transport
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2016-06-30
    Description: Foreign DNA molecules and chromosomal fragments are generally eliminated from proliferating cells, but we know little about how mammalian cells prevent their propagation. Here, we show that dividing human and canine cells partition transfected plasmid DNA asymmetrically, preferentially into the daughter cell harboring the young centrosome. Independently of how they...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 9
    Publication Date: 2015-09-18
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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