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  • 1.
    Carlsson, Sven R
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Simonsen, Anne
    Membrane dynamics in autophagosome biogenesis2015In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 128, no 2, p. 193-205Article in journal (Other academic)
    Abstract [en]

    Bilayered phospholipid membranes are vital to the organization of the living cell. Based on fundamental principles of polarity, membranes create borders allowing defined spaces to be encapsulated. This compartmentalization is a prerequisite for the complex functional design of the eukaryotic cell, yielding localities that can differ in composition and operation. During macroautophagy, cytoplasmic components become enclosed by a growing double bilayered membrane, which upon closure creates a separate compartment, the autophagosome. The autophagosome is then primed for fusion with endosomal and lysosomal compartments, leading to degradation of the captured material. A large number of proteins have been found to be essential for autophagy, but little is known about the specific lipids that constitute the autophagic membranes and the membrane modeling events that are responsible for regulation of autophagosome shape and size. In this Commentary, we review the recent progress in our understanding of the membrane shaping and remodeling events that are required at different steps of the autophagy pathway.

  • 2.
    Carlsson, Sven R
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Simonsen, Anne
    Recycling endosomes and autophagy2015In: Cell Technology (Saibou Kougaku), Vol. 34, no 2, p. 138-142Article in journal (Other academic)
  • 3.
    Elluri, Sridhar
    et al.
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS). Division of Pathophysiology, National Institute of Cholera and Enteric Diseases, Kolkata, West Bengal, India.
    Enow Oben Ayuk, Constance
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
    Vdovikova, Svitlana
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
    Rompikuntal, Pramod K
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
    Dongre, Mitesh
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
    Carlsson, Sven
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Pal, Amit
    Division of Pathophysiology, National Institute of Cholera and Enteric Diseases, Kolkata, West Bengal, India.
    Uhlin, Bernt Eric
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
    Wai, Sun Nyunt
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
    Outer membrane vesicles mediate transport of biologically active Vibrio cholerae cytolysin (VCC) from V. cholerae strains2014In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 9, no 9, p. e106731-Article in journal (Refereed)
    Abstract [en]

    Background Outer membrane vesicles (OMVs) released from Gram-negative bacteria can serve as vehicles for the translocation of virulence factors. Vibrio cholerae produce OMVs but their putative role in translocation of effectors involved in pathogenesis has not been well elucidated. The V. cholerae cytolysin (VCC), is a pore-forming toxin that lyses target eukaryotic cells by forming transmembrane oligomeric β-barrel channels. It is considered a potent toxin that contributes to V. cholerae pathogenesis. The mechanisms involved in the secretion and delivery of the VCC have not been extensively studied.

    Methodology/Principal Findings OMVs from V. cholerae strains were isolated and purified using a differential centrifugation procedure and Optiprep centrifugation. The ultrastructure and the contents of OMVs were examined under the electron microscope and by immunoblot analyses respectively. We demonstrated that VCC from V. cholerae strain V:5/04 was secreted in association with OMVs and the release of VCC via OMVs is a common feature among V. cholerae strains. The biological activity of OMV-associated VCC was investigated using contact hemolytic assay and epithelial cell cytotoxicity test. It showed toxic activity on both red blood cells and epithelial cells. Our results indicate that the OMVs architecture might play a role in stability of VCC and thereby can enhance its biological activities in comparison with the free secreted VCC. Furthermore, we tested the role of OMV-associated VCC in host cell autophagy signalling using confocal microscopy and immunoblot analysis. We observed that OMV-associated VCC triggered an autophagy response in the target cell and our findings demonstrated for the first time that autophagy may operate as a cellular defence mechanism against an OMV-associated bacterial virulence factor.

    Conclusion/Significance Biological assays of OMVs from the V. cholerae strain V:5/04 demonstrated that OMV-associated VCC is indeed biologically active and induces toxicity on mammalian cells and furthermore can induce autophagy.

  • 4. Holland, Petter
    et al.
    Knaevelsrud, Helene
    Soreng, Kristiane
    Mathai, Benan J.
    Lystad, Alf Hakon
    Pankiv, Serhiy
    Bjorndal, Gunnveig T.
    Schultz, Sebastian W.
    Lobert, Viola H.
    Chan, Robin B.
    Zhou, Bowen
    Liestol, Knut
    Carlsson, Sven R.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Melia, Thomas J.
    Di Paolo, Gilbert
    Simonsen, Anne
    HS1BP3 negatively regulates autophagy by modulation of phosphatidic acid levels2016In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 7, article id 13889Article in journal (Refereed)
    Abstract [en]

    A fundamental question is how autophagosome formation is regulated. Here we show that the PX domain protein HS1BP3 is a negative regulator of autophagosome formation. HS1BP3 depletion increased the formation of LC3-positive autophagosomes and degradation of cargo both in human cell culture and in zebrafish. HS1BP3 is localized to ATG16L1-and ATG9-positive autophagosome precursors and we show that HS1BP3 binds phosphatidic acid (PA) through its PX domain. Furthermore, we find the total PA content of cells to be significantly upregulated in the absence of HS1BP3, as a result of increased activity of the PA-producing enzyme phospholipase D (PLD) and increased localization of PLD1 to ATG16L1-positive membranes. We propose that HS1BP3 regulates autophagy by modulating the PA content of the ATG16L1-positive autophagosome precursor membranes through PLD1 activity and localization. Our findings provide key insights into how autophagosome formation is regulated by a novel negative-feedback mechanism on membrane lipids.

  • 5. Holmfeldt, Per
    et al.
    Brännström, Kristoffer
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
    Sellin, Mikael E
    Segerman, Bo
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Gullberg, Martin
    The Schistosoma mansoni protein SM16/SmSLP/SmSPO-1 is a membrane-binding protein that lacks the proposed microtubule-regulatory activity2007In: Molecular and biochemical parasitology (Print), ISSN 0166-6851, E-ISSN 1872-9428, Vol. 156, no 2, p. 225-234Article in journal (Refereed)
  • 6.
    Håberg, Karin
    et al.
    Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
    Lundmark, Richard
    Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
    Carlsson, Sven
    Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
    SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking.2008In: Journal of Cell Science, ISSN 0021-9533, Vol. 121, no Pt 9, p. 1495-505Article in journal (Refereed)
  • 7. Klionsky, Daniel J.
    et al.
    Carlsson, Sven R.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Zughaier, Susu M.
    Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)2016In: Autophagy, ISSN 1554-8627, E-ISSN 1554-8635, Vol. 12, no 1, p. 1-222Article in journal (Refereed)
  • 8.
    Knævelsrud, Helene
    et al.
    Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Simonsen, Anne
    Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
    SNX18 tubulates recycling endosomes for autophagosome biogenesis2013In: Autophagy, ISSN 1554-8627, E-ISSN 1554-8635, ISSN 1554-8635 (online), Vol. 9, no 10, p. 1639-1641Article in journal (Refereed)
    Abstract [en]

    The role of membrane remodeling and phosphoinositide-binding proteins in autophagy remains elusive. PX domain proteins bind phosphoinositides and participate in membrane remodeling and trafficking events and we therefore hypothesized that one or several PX domain proteins are involved in autophagy. Indeed, the PX-BAR protein SNX18 was identified as a positive regulator of autophagosome formation using an image-based siRNA screen. We show that SNX18 interacts with ATG16L1 and LC3, and functions downstream of ATG14 and the class III PtdIns3K complex in autophagosome formation. SNX18 facilitates recruitment of ATG16L1 to perinuclear recycling endosomes, and its overexpression leads to tubulation of ATG16L1- and LC3-positive membranes. We propose that SNX18 promotes LC3 lipidation and tubulation of recycling endosomes to provide membrane for phagophore expansion.

  • 9.
    Knævelsrud, Helene
    et al.
    University of Oslo, Institute of Basic Medical Sciences.
    Håberg, Karin
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Søreng, Kristiane
    University of Oslo, Institute of Basic Medical Sciences.
    Rasmuson, Fredrik
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Raiborg, Camilla
    University of Oslo, Centre for Cancer Biomedicine; Oslo University Hospital, Institute for Cancer Research, Department of Biochemistry.
    Liestøl, Knut
    University of Oslo, Centre for Cancer Biomedicine.
    Stenmark, Harald
    University of Oslo, Centre for Cancer Biomedicine; Oslo University Hospital, Institute for Cancer Research, Department of Biochemistry.
    Carlsson, Sven
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Simonsen, Anne
    University of Oslo, Institute of Basic Medical Sciences.
    The membrane-remodeling PX-BAR protein SNX18 is required for autophagyManuscript (preprint) (Other academic)
    Abstract [en]

    Autophagy is a catabolic pathway targeting cytoplasmic material for lysosomal degradation,thereby protecting cells from accumulation of toxic components and enabling cells to survivescarce nutrient supplies. Macroautophagy is characterized by the sequestration of cytoplasmicmaterial into double-membrane vesicles, but the membrane remodeling events required forformation of autophagic vesicles are still not completely understood. However, the class IIIphosphatidylinositol 3-kinase (PI3K)/Vps34 complex and phosphatidylinositol-3-phosphate(PI3P) are of core importance to induction of autophagy. Since PX domain containingproteins are known to bind PI3P and other phosphoinositides and mediate membraneremodeling and trafficking events, we performed an imaging-based siRNA screen targetingPX domain proteins using formation of GFP-LC3 positive autophagosomes as a read-out.The PX-BAR protein SNX18 was found to strongly inhibit autophagosome formation. In linewith this, overexpression of SNX18 increased LC3 lipidation and GFP-LC3 spot formationand we demonstrate that membrane binding of SNX18 is required for efficientautophagosome formation. Moreover, SNX18 colocalizes and interacts with the autophagyassociatedproteins LC3 and TBK1. Our study identified the PX-BAR protein SNX18 to beinvolved in membrane events required for autophagosome formation.

  • 10. Knævelsrud, Helene
    et al.
    Søreng, Kristiane
    Raiborg, Camilla
    Håberg, Karin
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Rasmuson, Fredrik
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Brech, Andreas
    Liestøl, Knut
    Rusten, Tor Erik
    Stenmark, Harald
    Neufeld, Thomas P
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Simonsen, Anne
    Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation2013In: Journal of Cell Biology, ISSN 0021-9525, E-ISSN 1540-8140, Vol. 202, no 2, p. 331-349Article in journal (Refereed)
    Abstract [en]

    The membrane remodeling events required for autophagosome biogenesis are still poorly understood. Because PX domain proteins mediate membrane remodeling and trafficking, we conducted an imaging-based siRNA screen for autophagosome formation targeting human PX proteins. The PX-BAR protein SNX18 was identified as a positive regulator of autophagosome formation, and its Drosophila melanogaster homologue SH3PX1 was found to be required for efficient autophagosome formation in the larval fat body. We show that SNX18 is required for recruitment of Atg16L1-positive recycling endosomes to a perinuclear area and for delivery of Atg16L1- and LC3-positive membranes to autophagosome precursors. We identify a direct interaction of SNX18 with LC3 and show that the pro-autophagic activity of SNX18 depends on its membrane binding and tubulation capacity. We also show that the function of SNX18 in membrane tubulation and autophagy is negatively regulated by phosphorylation of S233. We conclude that SNX18 promotes autophagosome formation by virtue of its ability to remodel membranes and provide membrane to forming autophagosomes.

  • 11.
    Lundmark, Richard
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components2003In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 278, no 47, p. 46772-46781Article in journal (Refereed)
    Abstract [en]

    Sorting nexin 9 (SNX9) belongs to a family of proteins, the sorting nexins, that are characterized by the presence of a subclass of the phosphoinositide-binding phox domain. SNX9 has in its amino terminus a Src homology 3 domain and a region with predicted low complexity followed by a carboxyl-terminal part containing the phox domain. We previously found that SNX9 is one of the major proteins in hematopoietic cells that binds to the alpha and beta2-appendages of adaptor protein complex 2 (AP-2), a protein with a critical role in the formation of clathrin-coated vesicles at the plasma membrane. In the present study we show that clathrin and dynamin-2, two other essential molecules in the endocytic process, also interact with SNX9. We found that both AP-2 and clathrin bind to the low complexity region in SNX9 in a cooperative manner, whereas dynamin-2 binds to the Src homology 3 domain. In the cytosol, SNX9 is present in a 14.5 S complex containing dynamin-2 and an unidentified 41-kDa protein. In HeLa cells, SNX9 co-localized with both AP-2 and dynamin-2 at the plasma membrane or on vesicular structures derived from it but not with the early endosomal marker EEA1 or with AP-1. The results suggest that SNX9 may be recruited together with dynamin-2 and become co-assembled with AP-2 and clathrin at the plasma membrane. Overexpression in both K562 and HeLa cells of truncated forms of SNX9 interfered with the uptake of transferrin, consistent with a role of SNX9 in endocytosis.

  • 12.
    Lundmark, Richard
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    The beta-appendages of the four adaptor-protein (AP) complexes: structure and binding properties, and identification of sorting nexin 9 as an accessory protein to AP-22002In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 362, no 3, p. 597-607Article in journal (Refereed)
    Abstract [en]

    Adaptor protein (AP) complexes are essential components for the formation of coated vesicles and the recognition of cargo proteins for intracellular transport. Each AP complex exposes two appendage domains with that function to bind regulatory accessory proteins in the cytosol. Secondary structure predictions, sequence alignments and CD spectroscopy were used to relate the beta-appendages of all human AP complexes to the previously published crystal structure of AP-2. The results suggested that the beta-appendages of AP-1, AP-2 and AP-3 have similar structures, consisting of two subdomains, whereas that of AP-4 lacks the inner subdomain. Pull-down and overlay assays showed partial overlap in the binding specificities of the beta-appendages of AP-1 and AP-2, whereas the corresponding domain of AP-3 displayed a unique binding pattern. That AP-4 may have a truncated, non-functional domain was indicated by its apparent inability to bind any proteins from cytosol. Of several novel beta-appendage-binding proteins detected, one that had affinity exclusively for AP-2 was identified as sorting nexin 9 (SNX9). SNX9, which contains a phox and an Src homology 3 domain, was found in large complexes and was at least partially associated with AP-2 in the cytosol. SNX9 may function to assist AP-2 in its role at the plasma membrane.

  • 13.
    Lundmark, Richard
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Driving membrane curvature in clathrin-dependent and clathrin-independent endocytosis.2010In: Seminars in Cell and Developmental Biology, ISSN 1084-9521, E-ISSN 1096-3634, Vol. 21, no 4, p. 363-70Article in journal (Refereed)
    Abstract [en]

    Cellular activity depends to a large extent on membrane bilayer dynamics. Many processes, such as organelle biogenesis and vesicular transport, rely on alterations in membrane structure and shape. It is now widely accepted that intracellular membrane curvature generation and remodelling is mediated and regulated by protein action, and the mechanisms behind the processes are currently being revealed. Here, we will briefly discuss the key principles of membrane deformation and focus on different endocytic events that use various kinds of proteins to shape the plasma membrane into transport carriers. The entry routes are adopted to make sure that a vast variety of molecules on the cell surface can be regulated by endocytosis. The principles for membrane sculpting of endocytic carriers can be viewed either from a perspective of rigid coat budding or of flexible opportunistic budding. We will discuss these principles and their implications, focusing on clathrin-dependent and -independent carrier formation and the proteins involved in the respective pathways.

  • 14.
    Lundmark, Richard
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Expression and properties of sorting nexin 9 in dynamin-mediated endocytosis2005In: Methods in Enzymology, ISSN 0076-6879, E-ISSN 1557-7988, Vol. 404, p. 545-556Article in journal (Refereed)
    Abstract [en]

    Sorting nexin 9 (SNX9) is identified as an important regulator of dynamin function in clathrin-mediated endocytosis. SNX9 recruits dynamin to the plasma membrane and promotes its GTPase activity, resulting in membrane constriction and ultimate transport vesicle scission. This chapter describes procedures to express recombinant SNX9, to biochemically characterize the cytosolic complex between SNX9 and dynamin, and to identify additional interacting partners of SNX9. Assays are presented to investigate the requirements for SNX9-dependent membrane recruitment of dynamin in vitro and in vivo.

  • 15.
    Lundmark, Richard
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Regulated membrane recruitment of dynamin-2 mediated by sorting nexin 9.2004In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 279, no 41, p. 42694-42702Article in journal (Refereed)
    Abstract [en]

    The endocytic proteins sorting nexin 9 (SNX9) and dynamin-2 (Dyn2) assemble in the cytosol as a resting complex, together with a 41-kDa protein. We show here that the complex can be activated for membrane binding of SNX9 and Dyn2 by incubation of cytosol in the presence of ATP. SNX9 was essential for Dyn2 recruitment, whereas the reverse was not the case. RNA interference experiments confirmed that SNX9 functions as a mediator of Dyn2 recruitment to membranes in cells. The 41-kDa component was identified as the glycolytic enzyme aldolase. Aldolase bound with high affinity to a tryptophan-containing acidic sequence in SNX9 located close to its Phox homology domain, thereby blocking the membrane binding activity of SNX9. Phosphorylation of SNX9 released aldolase from the native cytosolic complex and rendered SNX9 competent for membrane binding. The results suggest that SNX9-dependent recruitment of Dyn2 to the membrane is regulated by an interaction between SNX9 and aldolase.

  • 16.
    Lundmark, Richard
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    SNX9 - a prelude to vesicle release2009In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 122, no 1, p. 5-11Article in journal (Refereed)
    Abstract [en]

    The sorting nexin SNX9 has, in the past few years, been singled out as an important protein that participates in fundamental cellular activities. SNX9 binds strongly to dynamin and is partly responsible for the recruitment of this GTPase to sites of endocytosis. SNX9 also has a high capacity for modulation of the membrane and might therefore participate in the formation of the narrow neck of endocytic vesicles before scission occurs. Once assembled on the membrane, SNX9 stimulates the GTPase activity of dynamin to facilitate the scission reaction. It has also become clear that SNX9 has the ability to activate the actin regulator N-WASP in a membrane-dependent manner to coordinate actin polymerization with vesicle release. In this Commentary, we summarize several aspects of SNX9 structure and function in the context of membrane remodeling, discuss its interplay with various interaction partners and present a model of how SNX9 might work in endocytosis.

  • 17. Marchès, O
    et al.
    Batchelor, M
    Shaw, RK
    Patel, A
    Cummings, N
    Nagai, T
    Sasakawa, C
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Lundmark, Richard
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Cougoule, C
    Caron, E
    Knutton, S
    Connerton, I
    Frankel, G
    EspF of enteropathogenic Escherichia coli binds sorting nexin 92006In: Journal of Bacteriology, Vol. 188, no 8, p. 3110-3115Article in journal (Refereed)
  • 18.
    Olofsson, Annelie
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Bäckström, AnnaUmeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.Petzold, KatjajUmeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.Gröbner, GerhardUmeå University, Faculty of Science and Technology, Department of Chemistry.Wai, SNUmeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).Carlsson, SvenUmeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.Schleucher, JürgenUmeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.Arnqvist, AnnaUmeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Helicobacter pylori outer membrane vesicles and properties for intimate host interactions2007Conference proceedings (editor) (Refereed)
  • 19.
    Olofsson, Annelie
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Vallström, Anna
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Petzold, Katja
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Schleucher, Jürgen
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Haas, Rainer
    Max-von-Pettenkofer-Institute of Hygiene and Medical Microbiology, Dept of Bacteriology, Munich, Germany.
    Backert, Steffen
    School of Biomolecular and Biomedical Sciences, University College Dublin, Ireland.
    Nyunt Wai, Sun
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
    Gröbner, Gerhard
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Arnqvist, Anna
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Characterization of Helicobacter pylori vesicles and their cognate properties for intimate host interactionsManuscript (preprint) (Other academic)
  • 20.
    Olofsson, Annelie
    et al.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Vallström, Anna
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics. Umeå University, Faculty of Medicine, Department of Odontology, Oral Microbiology.
    Petzold, Katja
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Tegtmeyer, Nicole
    Schleucher, Jürgen
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Haas, Rainer
    Backert, Steffen
    Wai, Sun Nyunt
    Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
    Gröbner, Gerhard
    Umeå University, Faculty of Science and Technology, Department of Chemistry.
    Arnqvist, Anna
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Biochemical and functional characterization of Helicobacter pylori vesicles2010In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 77, no 6, p. 1539-1555Article in journal (Refereed)
    Abstract [en]

    Helicobacter pylori can cause peptic ulcer disease and/or gastric cancer. Adhesion of bacteria to the stomach mucosa is an important contributor to the vigor of infection and resulting virulence. H. pylori adheres primarily via binding of BabA adhesins to ABO/Lewis b (Leb) blood group antigens and the binding of SabA adhesins to sialyl-Lewis x/a (sLex/a) antigens. Similar to most Gram-negative bacteria, H. pylori continuously buds off vesicles and vesicles derived from pathogenic bacteria often include virulence-associated factors. Here we biochemically characterized highly purified H. pylori vesicles. Major protein and phospholipid components associated with the vesicles were identified with mass spectroscopy and NMR. A subset of virulence factors present was confirmed by immunoblots. Additional functional and biochemical analysis focused on the vesicle BabA and SabA adhesins and their respective interactions to human gastric epithelium. Vesicles exhibit heterogeneity in their protein composition, which were specifically studied in respect to the BabA adhesin. We also demonstrate that the oncoprotein, CagA, is associated with the surface of H. pylori vesicles. Thus, we have explored mechanisms for intimate H. pylori vesicle-host interactions and found that the vesicles carry effector-promoting properties that are important to disease development.

  • 21. Pylypenko, Olena
    et al.
    Ignatev, Alexander
    Lundmark, Richard
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Rasmuson, Erika
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Rak, Alexey
    A combinatorial approach to crystallization of PX-BAR unit of the human Sorting Nexin 9.2008In: Journal of Structural Biology, ISSN 1047-8477, Vol. 162, no 2, p. 356-360Article in journal (Refereed)
  • 22. Pylypenko, Olena
    et al.
    Lundmark, Richard
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Rasmuson, Erika
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Rak, Alexey
    The PX-BAR membrane-remodeling unit of sorting nexin 9.2007In: EMBO Journal, ISSN 1460-2075, Vol. 26, no 22, p. 4788-800Article in journal (Refereed)
  • 23. Søreng, Kristiane
    et al.
    Munson, Michael J.
    Lamb, Christopher A.
    Bjørndal, Gunnveig T.
    Pankiv, Serhiy
    Carlsson, Sven R.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Tooze, Sharon A.
    Simonsen, Anne
    SNX18 regulates ATG9A trafficking from recycling endosomes by recruiting Dynamin-22018In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 19, no 4, article id e44837Article in journal (Refereed)
    Abstract [en]

    Trafficking of mammalian ATG9A between the Golgi apparatus, endosomes and peripheral ATG9A compartments is important for autophagosome biogenesis. Here, we show that the membrane remodelling protein SNX18, previously identified as a positive regulator of autophagy, regulates ATG9A trafficking from recycling endosomes. ATG9A is recruited to SNX18-induced tubules generated from recycling endosomes and accumulates in juxtanuclear recycling endosomes in cells lacking SNX18. Binding of SNX18 to Dynamin-2 is important for ATG9A trafficking from recycling endosomes and for formation of ATG16L1- and WIPI2-positive autophagosome precursor membranes. We propose a model where upon autophagy induction, SNX18 recruits Dynamin-2 to induce budding of ATG9A and ATG16L1 containing membranes from recycling endosomes that traffic to sites of autophagosome formation.

  • 24. van Weering, Jan R. T.
    et al.
    Sessions, Richard B.
    Traer, Colin J.
    Kloer, Daniel P.
    Bhatia, Vikram K.
    Stamou, Dimitrios
    Carlsson, Sven R.
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    Hurley, James H.
    Cullen, Peter J.
    Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules2012In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 31, no 23, p. 4466-4480Article in journal (Refereed)
    Abstract [en]

    Sorting nexins (SNXs) are regulators of endosomal sorting. For the SNX-BAR subgroup, a Bin/Amphiphysin/Rvs (BAR) domain is vital for formation/stabilization of tubular subdomains that mediate cargo recycling. Here, by analysing the in vitro membrane remodelling properties of all 12 human SNX-BARs, we report that some, but not all, can elicit the formation of tubules with diameters that resemble sorting tubules observed in cells. We reveal that SNX-BARs display a restricted pattern of BAR domain-mediated dimerization, and by resolving a 2.8 angstrom structure of a SNX1-BAR domain homodimer, establish that dimerization is achieved in part through neutralization of charged residues in the hydrophobic BAR-dimerization interface. Membrane remodelling also requires functional amphipathic helices, predicted to be present in all SNX-BARs, and the formation of high order SNX-BAR oligomers through selective 'tip-loop' interactions. Overall, the restricted and selective nature of these interactions provide a molecular explanation for how distinct SNX-BAR-decorated tubules are nucleated from the same endosomal vacuole, as observed in living cells. Our data provide insight into the molecular mechanism that generates and organizes the tubular endosomal network.

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