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  1. Article: A Case for Sec61 Channel Involvement in ERAD.

    Römisch, Karin

    Trends in biochemical sciences

    2017  Volume 42, Issue 3, Page(s) 171–179

    Abstract: Proteins that misfold in the endoplasmic reticulum (ER) need to be transported back to the cytosol for degradation by proteasomes, a process known as ER-associated degradation (ERAD). The first candidate discussed as a retrograde protein transport ... ...

    Abstract Proteins that misfold in the endoplasmic reticulum (ER) need to be transported back to the cytosol for degradation by proteasomes, a process known as ER-associated degradation (ERAD). The first candidate discussed as a retrograde protein transport conduit was the Sec61 channel which is responsible for secretory protein transport into the ER during biogenesis. The Sec61 channel binds the proteasome 19S regulatory particle which can extract an ERAD substrate from the ER. Nevertheless its role as a general export channel has been dismissed, and Hrd1 and Der1 have been proposed as alternatives. The discovery of export-specific sec61 mutants and of mammalian ERAD substrates whose export is dependent on the 19S regulatory particle suggest that dismissal of a role of Sec61 in export may have been premature.
    MeSH term(s) Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation/physiology ; Humans ; Proteasome Endopeptidase Complex/metabolism ; SEC Translocation Channels/genetics ; SEC Translocation Channels/metabolism
    Chemical Substances SEC Translocation Channels ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; 26S proteasome non-ATPase regulatory subunit 13 (EC 3.6.1.-)
    Language English
    Publishing date 2017-03
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2016.10.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1207: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Effect of Sec62 on the conformation of the Sec61 channel in yeast.

    Bhadra, Pratiti / Römisch, Karin / Helms, Volkhard

    Biochimica et biophysica acta. Biomembranes

    2022  Volume 1864, Issue 12, Page(s) 184050

    Abstract: Most eukaryotic secretory and membrane proteins are funneled by the Sec61 complex into the secretory pathway. Furthermore, some substrate peptides rely on two essential accessory proteins, Sec62 and Sec63, being present to assist with their translocation ...

    Abstract Most eukaryotic secretory and membrane proteins are funneled by the Sec61 complex into the secretory pathway. Furthermore, some substrate peptides rely on two essential accessory proteins, Sec62 and Sec63, being present to assist with their translocation via the Sec61 channel in post-translational translocation. Cryo-electron microscopy (cryo-EM) recently succeeded in determining atomistic structures of unbound and signal sequence-engaged Sec complexes from Saccharomyces cerevisiae, involving the Sec61 channel and the proteins Sec62, Sec63, Sec71 and Sec72. In this study, we investigated the conformational effects of Sec62 on Sec61. Indeed, we observed in molecular dynamics simulations that the conformational dynamics of lateral gate, plug and pore region of Sec61 are altered by the presence/absence of Sec62. In molecular dynamics simulations that were started from the cryo-EM structures of Sec61 coordinated to Sec62 or of apo Sec61, we observed that the luminal side of the lateral gate gradually adopts a closed conformation similar to the apo state during unbound state simulations. In contrast, it adopts a wider conformation in the bound state. Furthermore, we demonstrate that the conformation of the active (substrate-bound) state of the Sec61 channel shifts toward an alternative conformation in the absence of the substrate. We suggest that the signal peptide holds/stabilizes the active state conformation of Sec61 during post-translational translocation. Thus, our study explains the effect of Sec62 on the conformation of the Sec61 channel and describes the conformational transitions of Sec61 channel.
    MeSH term(s) Cryoelectron Microscopy ; Endoplasmic Reticulum/metabolism ; Heat-Shock Proteins/chemistry ; Membrane Proteins/chemistry ; Membrane Transport Proteins/metabolism ; Protein Sorting Signals ; Protein Transport ; SEC Translocation Channels/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Heat-Shock Proteins ; Membrane Proteins ; Membrane Transport Proteins ; Protein Sorting Signals ; SEC Translocation Channels ; SEC61 protein, S cerevisiae ; SEC62 protein, S cerevisiae ; SEC63 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2022-09-16
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2022.184050
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Book ; Online: Faculty Opinions recommendation of School closure and management practices during coronavirus outbreaks including COVID-19

    Romisch, Karin

    Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature

    a rapid systematic review.

    2020  

    Keywords covid19
    Publisher Faculty Opinions Ltd
    Publishing country uk
    Document type Book ; Online
    DOI 10.3410/f.737698180.793574118
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article: A Case for Sec61 Channel Involvement in ERAD

    Römisch, Karin

    Trends in biochemical sciences. 2017 Mar., v. 42, no. 3

    2017  

    Abstract: Proteins that misfold in the endoplasmic reticulum (ER) need to be transported back to the cytosol for degradation by proteasomes, a process known as ER-associated degradation (ERAD). The first candidate discussed as a retrograde protein transport ... ...

    Abstract Proteins that misfold in the endoplasmic reticulum (ER) need to be transported back to the cytosol for degradation by proteasomes, a process known as ER-associated degradation (ERAD). The first candidate discussed as a retrograde protein transport conduit was the Sec61 channel which is responsible for secretory protein transport into the ER during biogenesis. The Sec61 channel binds the proteasome 19S regulatory particle which can extract an ERAD substrate from the ER. Nevertheless its role as a general export channel has been dismissed, and Hrd1 and Der1 have been proposed as alternatives. The discovery of export-specific sec61 mutants and of mammalian ERAD substrates whose export is dependent on the 19S regulatory particle suggest that dismissal of a role of Sec61 in export may have been premature.
    Keywords biogenesis ; cytosol ; endoplasmic reticulum ; mammals ; mutants ; proteasome endopeptidase complex ; transport proteins
    Language English
    Dates of publication 2017-03
    Size p. 171-179.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 194220-7
    ISSN 0968-0004 ; 0376-5067
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2016.10.005
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 78/716: Show issues

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  5. Article ; Online: How does Sec63 affect the conformation of Sec61 in yeast?

    Bhadra, Pratiti / Yadhanapudi, Lalitha / Römisch, Karin / Helms, Volkhard

    PLoS computational biology

    2021  Volume 17, Issue 3, Page(s) e1008855

    Abstract: The Sec complex catalyzes the translocation of proteins of the secretory pathway into the endoplasmic reticulum and the integration of membrane proteins into the endoplasmic reticulum membrane. Some substrate peptides require the presence and involvement ...

    Abstract The Sec complex catalyzes the translocation of proteins of the secretory pathway into the endoplasmic reticulum and the integration of membrane proteins into the endoplasmic reticulum membrane. Some substrate peptides require the presence and involvement of accessory proteins such as Sec63. Recently, a structure of the Sec complex from Saccharomyces cerevisiae, consisting of the Sec61 channel and the Sec62, Sec63, Sec71 and Sec72 proteins was determined by cryo-electron microscopy (cryo-EM). Here, we show by co-precipitation that the Sec61 channel subunit Sbh1 is not required for formation of stable Sec63-Sec61 contacts. Molecular dynamics simulations started from the cryo-EM conformation of Sec61 bound to Sec63 and of unbound Sec61 revealed how Sec63 affects the conformation of Sec61 lateral gate, plug, pore region and pore ring diameter via three intermolecular contact regions. Molecular docking of SRP-dependent vs. SRP-independent signal peptide chains into the Sec61 channel showed that the pore regions affected by presence/absence of Sec63 play a crucial role in positioning the signal anchors of SRP-dependent substrates nearby the lateral gate.
    MeSH term(s) Cryoelectron Microscopy ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/metabolism ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Conformation ; SEC Translocation Channels/chemistry ; SEC Translocation Channels/metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Sepharose/analogs & derivatives ; Sepharose/chemistry ; Sepharose/metabolism
    Chemical Substances Heat-Shock Proteins ; Membrane Transport Proteins ; SEC Translocation Channels ; SEC61 protein, S cerevisiae ; SEC63 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; concanavalin A-sepharose ; Sepharose (9012-36-6)
    Language English
    Publishing date 2021-03-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2193340-6
    ISSN 1553-7358 ; 1553-734X
    ISSN (online) 1553-7358
    ISSN 1553-734X
    DOI 10.1371/journal.pcbi.1008855
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Book ; Online ; Thesis: Regulation of protein transport into the ER by phosphorylation of Sbh1/Sec61β

    Guido, Barbieri [Verfasser] / Römisch, Karin [Akademischer Betreuer]

    2022  

    Author's details Barbieri Guido ; Betreuer: Karin Römisch
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Saarländische Universitäts- und Landesbibliothek
    Publishing place Saarbrücken
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  7. Article: Diversion at the ER: How Plasmodium falciparum exports proteins into host erythrocytes.

    Römisch, Karin

    F1000Research

    2012  Volume 1, Page(s) 12

    Abstract: Malaria is caused by parasites which live in host erythrocytes and remodel these cells to provide optimally for the parasites' needs by exporting effector proteins into the host cells. Eight years ago the discovery of a host cell targeting sequence ... ...

    Abstract Malaria is caused by parasites which live in host erythrocytes and remodel these cells to provide optimally for the parasites' needs by exporting effector proteins into the host cells. Eight years ago the discovery of a host cell targeting sequence present in both soluble and transmembrane  P. falciparum exported proteins generated a starting point for investigating the mechanism of parasite protein transport into infected erythrocytes. Since then many confusing facts about this targeting signal have emerged. In this paper, I try to make sense of them.
    Language English
    Publishing date 2012
    Publishing country England
    Document type Journal Article
    ZDB-ID 2699932-8
    ISSN 2046-1402
    ISSN 2046-1402
    DOI 10.12688/f1000research.1-12.v2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Book ; Thesis: Zur Geschichte der Schwangerenfürsorge der Berliner Gesundheitsämter

    Römisch, Karin

    1984  

    Size 167 S. : graph. Darst.
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Berlin, Freie Univ., Diss., 1984
    HBZ-ID HT003261409
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    86 D 282 order for loan Magazin

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  9. Article ; Online: How does Sec63 affect the conformation of Sec61 in yeast?

    Pratiti Bhadra / Lalitha Yadhanapudi / Karin Römisch / Volkhard Helms

    PLoS Computational Biology, Vol 17, Iss 3, p e

    2021  Volume 1008855

    Abstract: The Sec complex catalyzes the translocation of proteins of the secretory pathway into the endoplasmic reticulum and the integration of membrane proteins into the endoplasmic reticulum membrane. Some substrate peptides require the presence and involvement ...

    Abstract The Sec complex catalyzes the translocation of proteins of the secretory pathway into the endoplasmic reticulum and the integration of membrane proteins into the endoplasmic reticulum membrane. Some substrate peptides require the presence and involvement of accessory proteins such as Sec63. Recently, a structure of the Sec complex from Saccharomyces cerevisiae, consisting of the Sec61 channel and the Sec62, Sec63, Sec71 and Sec72 proteins was determined by cryo-electron microscopy (cryo-EM). Here, we show by co-precipitation that the Sec61 channel subunit Sbh1 is not required for formation of stable Sec63-Sec61 contacts. Molecular dynamics simulations started from the cryo-EM conformation of Sec61 bound to Sec63 and of unbound Sec61 revealed how Sec63 affects the conformation of Sec61 lateral gate, plug, pore region and pore ring diameter via three intermolecular contact regions. Molecular docking of SRP-dependent vs. SRP-independent signal peptide chains into the Sec61 channel showed that the pore regions affected by presence/absence of Sec63 play a crucial role in positioning the signal anchors of SRP-dependent substrates nearby the lateral gate.
    Keywords Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2021-03-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: The ER Protein Translocation Channel Subunit Sbh1 Controls Virulence of Cryptococcus neoformans.

    Santiago-Tirado, Felipe H / Hurtaux, Thomas / Geddes-McAlister, Jennifer / Nguyen, Duy / Helms, Volkhard / Doering, Tamara L / Römisch, Karin

    mBio

    2023  Volume 14, Issue 1, Page(s) e0338422

    Abstract: The fungal pathogen Cryptococcus neoformans is distinguished by a cell-wall-anchored polysaccharide capsule that is critical for virulence. Biogenesis of both cell wall and capsule relies on the secretory pathway. Protein secretion begins with ... ...

    Abstract The fungal pathogen Cryptococcus neoformans is distinguished by a cell-wall-anchored polysaccharide capsule that is critical for virulence. Biogenesis of both cell wall and capsule relies on the secretory pathway. Protein secretion begins with polypeptide translocation across the endoplasmic reticulum (ER) membrane through a highly conserved channel formed by three proteins: Sec61, Sbh1, and Sss1. Sbh1, the most divergent, contains multiple phosphorylation sites, which may allow it to regulate entry into the secretory pathway in a species- and protein-specific manner. Absence of
    MeSH term(s) Animals ; Mice ; Cryptococcosis/microbiology ; Cryptococcus neoformans ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Mammals/metabolism ; Polysaccharides/metabolism ; Protein Transport ; Proteomics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; SEC Translocation Channels/genetics ; Translocation, Genetic ; Virulence ; Virulence Factors/genetics ; Virulence Factors/metabolism ; Endoplasmic Reticulum/metabolism
    Chemical Substances Fungal Proteins ; Polysaccharides ; Saccharomyces cerevisiae Proteins ; SEC Translocation Channels ; SSS1 protein, S cerevisiae ; Virulence Factors
    Language English
    Publishing date 2023-02-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.03384-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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