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  1. Article ; Online: ER exit sites--localization and control of COPII vesicle formation.

    Budnik, Annika / Stephens, David J

    FEBS letters

    2009  Volume 583, Issue 23, Page(s) 3796–3803

    Abstract: The first membrane trafficking step in the biosynthetic secretory pathway, the export of proteins and lipids from the endoplasmic reticulum (ER), is mediated by COPII-coated vesicles. In mammalian cells, COPII vesicle budding occurs at specialized sites ... ...

    Abstract The first membrane trafficking step in the biosynthetic secretory pathway, the export of proteins and lipids from the endoplasmic reticulum (ER), is mediated by COPII-coated vesicles. In mammalian cells, COPII vesicle budding occurs at specialized sites on the ER, the so-called transitional ER (tER). Here, we discuss aspects of the formation and maintenance of these sites, the mechanisms by which cargo becomes segregated within them, and the propagation of ER exit sites (ERES) during cell division. All of these features are inherently linked to the formation, maintenance and function of the Golgi apparatus underlining the importance of ERES to Golgi function and more widely in terms of intracellular organization and cellular function.
    MeSH term(s) Animals ; COP-Coated Vesicles/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Humans
    Language English
    Publishing date 2009-10-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2009.10.038
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 282: Show issues Location:
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  2. Article ; Online: Characterization of human Sec16B: indications of specialized, non-redundant functions.

    Budnik, Annika / Heesom, Kate J / Stephens, David J

    Scientific reports

    2011  Volume 1, Page(s) 77

    Abstract: The endoplasmic reticulum (ER) represents the entry point into the secretory pathway and from here newly synthesized proteins and lipids are delivered to the Golgi. The selective cargo export from the ER is mediated by COPII-assembly at specific sites of ...

    Abstract The endoplasmic reticulum (ER) represents the entry point into the secretory pathway and from here newly synthesized proteins and lipids are delivered to the Golgi. The selective cargo export from the ER is mediated by COPII-assembly at specific sites of the ER, the so-called transitional ER (tER). The peripheral membrane protein Sec16, first identified in yeast, localizes to transitional ER and plays a key role in organization of these sites. Sec16 defines the tER and is thought to act as a scaffold for the COPII coat assembly. In humans two isoforms of Sec16 are present, the larger Sec16A and the smaller Sec16B. Nevertheless, the functional differences between the two isoforms are ill-defined. Here we describe characterization of the localization and dynamics of Sec16B relative to Sec16A, provide evidence that Sec16B is likely a minor or perhaps specialized form of Sec16, and that it is not functionally redundant with Sec16A.
    MeSH term(s) Base Sequence ; DNA Primers ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/immunology ; DNA-Binding Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Green Fluorescent Proteins/genetics ; HeLa Cells ; Humans ; Polymerase Chain Reaction ; RNA Interference ; RNA, Small Interfering/genetics
    Chemical Substances DNA Primers ; DNA-Binding Proteins ; RNA, Small Interfering ; SEC16B protein, human ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2011-08-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep00077
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion.

    McCaughey, Janine / Miller, Victoria J / Stevenson, Nicola L / Brown, Anna K / Budnik, Annika / Heesom, Kate J / Alibhai, Dominic / Stephens, David J

    Cell reports

    2016  Volume 15, Issue 8, Page(s) 1648–1659

    Abstract: Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, ... ...

    Abstract Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export.
    MeSH term(s) Collagen/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Green Fluorescent Proteins/metabolism ; Humans ; Mannosidases/metabolism ; Models, Biological ; Protein Transport ; Proteins/metabolism ; RNA, Small Interfering/metabolism ; Reproducibility of Results
    Chemical Substances Proteins ; RNA, Small Interfering ; TFG protein, human ; Green Fluorescent Proteins (147336-22-9) ; Collagen (9007-34-5) ; Mannosidases (EC 3.2.1.-) ; mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase (EC 3.2.1.114)
    Language English
    Publishing date 2016-05-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2016.04.062
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: The Orphan Receptor Tie1 Controls Angiogenesis and Vascular Remodeling by Differentially Regulating Tie2 in Tip and Stalk Cells.

    Savant, Soniya / La Porta, Silvia / Budnik, Annika / Busch, Katrin / Hu, Junhao / Tisch, Nathalie / Korn, Claudia / Valls, Aida Freire / Benest, Andrew V / Terhardt, Dorothee / Qu, Xianghu / Adams, Ralf H / Baldwin, H Scott / Ruiz de Almodóvar, Carmen / Rodewald, Hans-Reimer / Augustin, Hellmut G

    Cell reports

    2015  Volume 12, Issue 11, Page(s) 1761–1773

    Abstract: Tie1 is a mechanistically poorly characterized endothelial cell (EC)-specific orphan receptor. Yet, Tie1 deletion is embryonic lethal and Tie1 has been implicated in critical vascular pathologies, including atherosclerosis and tumor angiogenesis. Here, ... ...

    Abstract Tie1 is a mechanistically poorly characterized endothelial cell (EC)-specific orphan receptor. Yet, Tie1 deletion is embryonic lethal and Tie1 has been implicated in critical vascular pathologies, including atherosclerosis and tumor angiogenesis. Here, we show that Tie1 does not function independently but exerts context-dependent effects on the related receptor Tie2. Tie1 was identified as an EC activation marker that is expressed during angiogenesis by a subset of angiogenic tip and remodeling stalk cells and downregulated in the adult quiescent vasculature. Functionally, Tie1 expression by angiogenic EC contributes to shaping the tip cell phenotype by negatively regulating Tie2 surface presentation. In contrast, Tie1 acts in remodeling stalk cells cooperatively to sustain Tie2 signaling. Collectively, our data support an interactive model of Tie1 and Tie2 function, in which dynamically regulated Tie1 versus Tie2 expression determines the net positive or negative effect of Tie1 on Tie2 signaling.
    MeSH term(s) Animals ; Cell Differentiation/physiology ; Cells, Cultured ; Embryonic Stem Cells/cytology ; Endothelial Cells/cytology ; Endothelial Cells/enzymology ; Mice ; Mice, Inbred C57BL ; Neovascularization, Physiologic/physiology ; Receptor, TIE-1/genetics ; Receptor, TIE-1/metabolism ; Receptor, TIE-1/physiology ; Receptor, TIE-2/genetics ; Receptor, TIE-2/metabolism ; Receptor, TIE-2/physiology ; Retinal Vessels/physiology ; Signal Transduction ; Vascular Remodeling/physiology
    Chemical Substances Receptor, TIE-1 (EC 2.7.10.1) ; Receptor, TIE-2 (EC 2.7.10.1)
    Language English
    Publishing date 2015-09-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2015.08.024
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Characteristic phenotypes associated with congenital dyserythropoietic anemia (type II) manifest at different stages of erythropoiesis.

    Satchwell, Timothy J / Pellegrin, Stephanie / Bianchi, Paola / Hawley, Bethan R / Gampel, Alexandra / Mordue, Kathryn E / Budnik, Annika / Fermo, Elisa / Barcellini, Wilma / Stephens, David J / van den Akker, Emile / Toye, Ashley M

    Haematologica

    2013  Volume 98, Issue 11, Page(s) 1788–1796

    Abstract: Congenital dyserythropoietic anemia type II is an autosomally recessive form of hereditary anemia caused by SEC23B gene mutations. Patients exhibit characteristic phenotypes including multinucleate erythroblasts, erythrocytes with hypoglycosylated ... ...

    Abstract Congenital dyserythropoietic anemia type II is an autosomally recessive form of hereditary anemia caused by SEC23B gene mutations. Patients exhibit characteristic phenotypes including multinucleate erythroblasts, erythrocytes with hypoglycosylated membrane proteins and an apparent double plasma membrane. Despite ubiquitous expression of SEC23B, the effects of mutations in this gene are confined to the erythroid lineage and the basis of this erythroid specificity remains to be defined. In addition, little is known regarding the stage at which the disparate phenotypes of this disease manifest during erythropoiesis. We employ an in vitro culture system to monitor the appearance of the defining phenotypes associated with congenital dyserythropoietic anemia type II during terminal differentiation of erythroblasts derived from small volumes of patient peripheral blood. Membrane protein hypoglycosylation was detected by the basophilic stage, preceding the onset of multinuclearity in orthochromatic erythroblasts that occurs coincident with the loss of secretory pathway proteins including SEC23A during erythropoiesis. Endoplasmic reticulum remnants were observed in nascent reticulocytes of both diseased and healthy donor cultures but were lost upon further maturation of normal reticulocytes, implicating a defect of ER clearance during reticulocyte maturation in congenital dyserythropoietic anemia type II. We also demonstrate distinct isoform and species-specific expression profiles of SEC23 during terminal erythroid differentiation and identify a prolonged expression of SEC23A in murine erythropoiesis compared to humans. We propose that SEC23A is able to compensate for the absence of SEC23B in mouse erythroblasts, providing a basis for the absence of phenotype within the erythroid lineage of a recently described SEC23B knockout mouse.
    MeSH term(s) Anemia, Dyserythropoietic, Congenital/genetics ; Anemia, Dyserythropoietic, Congenital/pathology ; Animals ; Cells, Cultured ; Erythropoiesis/physiology ; Humans ; Mice ; Mice, Inbred C57BL ; Phenotype
    Language English
    Publishing date 2013-08-09
    Publishing country Italy
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2333-4
    ISSN 1592-8721 ; 0017-6567 ; 0390-6078
    ISSN (online) 1592-8721
    ISSN 0017-6567 ; 0390-6078
    DOI 10.3324/haematol.2013.085522
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uh III Zs.76: Show issues Location:
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  6. Article: Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER

    Hughes, Helen / Budnik, Annika / Schmidt, Katy / Palmer, Krysten J / Mantell, Judith / Noakes, Chris / Johnson, Andrew / Carter, Deborah A / Verkade, Paul / Watson, Peter / Stephens, David J

    Journal of cell science. 2009 Aug. 15, v. 122, no. 16

    2009  

    Abstract: The COPII complex mediates the selective incorporation of secretory cargo and relevant machinery into budding vesicles at specialised sites on the endoplasmic reticulum membrane called transitional ER (tER). Here, we show using confocal microscopy, ... ...

    Abstract The COPII complex mediates the selective incorporation of secretory cargo and relevant machinery into budding vesicles at specialised sites on the endoplasmic reticulum membrane called transitional ER (tER). Here, we show using confocal microscopy, immunogold labelling of ultrathin cryosections and electron tomography that in human cells at steady state, Sec16 localises to cup-like structures of tER that are spatially distinct from the localisation of other COPII coat components. We show that Sec16 defines the tER, whereas Sec23-Sec24 and Sec13-Sec31 define later structures that precede but are distinct from the intermediate compartment. Steady-state localisation of Sec16 is independent of the localisation of downstream COPII components Sec23-Sec24 and Sec13-Sec31. Sec16 cycles on and off the membrane at a slower rate than other COPII components with a greater immobile fraction. We define the region of Sec16A that dictates its robust localisation of tER membranes and find that this requires both a highly charged region as well as a central domain that shows high sequence identity between species. The central conserved domain of Sec16 binds to Sec13 linking tER membrane localisation with COPII vesicle formation. These data are consistent with a model where Sec16 acts as a platform for COPII assembly at ERES.
    Language English
    Dates of publication 2009-0815
    Size p. 2924-2934.
    Publishing place The Company of Biologists Limited
    Document type Article
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    Database NAL-Catalogue (AGRICOLA)

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  7. Article: Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER.

    Hughes, Helen / Budnik, Annika / Schmidt, Katy / Palmer, Krysten J / Mantell, Judith / Noakes, Chris / Johnson, Andrew / Carter, Deborah A / Verkade, Paul / Watson, Peter / Stephens, David J

    Journal of cell science

    2009  Volume 122, Issue Pt 16, Page(s) 2924–2934

    Abstract: The COPII complex mediates the selective incorporation of secretory cargo and relevant machinery into budding vesicles at specialised sites on the endoplasmic reticulum membrane called transitional ER (tER). Here, we show using confocal microscopy, ... ...

    Abstract The COPII complex mediates the selective incorporation of secretory cargo and relevant machinery into budding vesicles at specialised sites on the endoplasmic reticulum membrane called transitional ER (tER). Here, we show using confocal microscopy, immunogold labelling of ultrathin cryosections and electron tomography that in human cells at steady state, Sec16 localises to cup-like structures of tER that are spatially distinct from the localisation of other COPII coat components. We show that Sec16 defines the tER, whereas Sec23-Sec24 and Sec13-Sec31 define later structures that precede but are distinct from the intermediate compartment. Steady-state localisation of Sec16 is independent of the localisation of downstream COPII components Sec23-Sec24 and Sec13-Sec31. Sec16 cycles on and off the membrane at a slower rate than other COPII components with a greater immobile fraction. We define the region of Sec16A that dictates its robust localisation of tER membranes and find that this requires both a highly charged region as well as a central domain that shows high sequence identity between species. The central conserved domain of Sec16 binds to Sec13 linking tER membrane localisation with COPII vesicle formation. These data are consistent with a model where Sec16 acts as a platform for COPII assembly at ERES.
    MeSH term(s) COP-Coated Vesicles/metabolism ; COP-Coated Vesicles/ultrastructure ; Endocytosis ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Fluorescence Recovery After Photobleaching ; Green Fluorescent Proteins/metabolism ; HeLa Cells ; Humans ; Kinetics ; Models, Biological ; Protein Binding ; Protein Subunits/metabolism ; Protein Transport ; Recombinant Fusion Proteins/metabolism ; Vesicular Transport Proteins/metabolism
    Chemical Substances Protein Subunits ; Recombinant Fusion Proteins ; SEC16A protein, human ; Vesicular Transport Proteins ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2009-07-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.044032
    Database MEDical Literature Analysis and Retrieval System OnLINE

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