Literature DB >> 23251026

Protein translocation across the rough endoplasmic reticulum.

Elisabet C Mandon1, Steven F Trueman, Reid Gilmore.   

Abstract

The rough endoplasmic reticulum is a major site of protein biosynthesis in all eukaryotic cells, serving as the entry point for the secretory pathway and as the initial integration site for the majority of cellular integral membrane proteins. The core components of the protein translocation machinery have been identified, and high-resolution structures of the targeting components and the transport channel have been obtained. Research in this area is now focused on obtaining a better understanding of the molecular mechanism of protein translocation and membrane protein integration.

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Year:  2013        PMID: 23251026      PMCID: PMC3552503          DOI: 10.1101/cshperspect.a013342

Source DB:  PubMed          Journal:  Cold Spring Harb Perspect Biol        ISSN: 1943-0264            Impact factor:   10.005


  154 in total

1.  BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane.

Authors:  K E Matlack; B Misselwitz; K Plath; T A Rapoport
Journal:  Cell       Date:  1999-05-28       Impact factor: 41.582

2.  Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP.

Authors:  D M Freymann; R J Keenan; R M Stroud; P Walter
Journal:  Nat Struct Biol       Date:  1999-08

3.  Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.

Authors:  K Plath; W Mothes; B M Wilkinson; C J Stirling; T A Rapoport
Journal:  Cell       Date:  1998-09-18       Impact factor: 41.582

4.  BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation.

Authors:  B D Hamman; L M Hendershot; A E Johnson
Journal:  Cell       Date:  1998-03-20       Impact factor: 41.582

5.  TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum.

Authors:  R S Hegde; S Voigt; T A Rapoport; V R Lingappa
Journal:  Cell       Date:  1998-03-06       Impact factor: 41.582

6.  Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms.

Authors:  E Wallin; G von Heijne
Journal:  Protein Sci       Date:  1998-04       Impact factor: 6.725

7.  In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli.

Authors:  H G Koch; T Hengelage; C Neumann-Haefelin; J MacFarlane; H K Hoffschulte; K L Schimz; B Mechler; M Müller
Journal:  Mol Biol Cell       Date:  1999-07       Impact factor: 4.138

8.  Shape of large bound polysomes in cultured fibroblasts and thyroid epithelial cells.

Authors:  A K Christensen; C M Bourne
Journal:  Anat Rec       Date:  1999-06-01

9.  A small particulate component of the cytoplasm.

Authors:  G E PALADE
Journal:  J Biophys Biochem Cytol       Date:  1955-01

10.  A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.

Authors:  S C Ogg; W P Barz; P Walter
Journal:  J Cell Biol       Date:  1998-07-27       Impact factor: 10.539

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  27 in total

1.  Interaction mapping of the Sec61 translocon identifies two Sec61α regions interacting with hydrophobic segments in translocating chains.

Authors:  Yuichiro Kida; Masao Sakaguchi
Journal:  J Biol Chem       Date:  2018-09-13       Impact factor: 5.157

Review 2.  Key roles of Arf small G proteins and biosynthetic trafficking for animal development.

Authors:  Francisco F Rodrigues; Tony J C Harris
Journal:  Small GTPases       Date:  2017-04-17

3.  Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.

Authors:  Alise J Ponsero; Aeid Igbaria; Maxwell A Darch; Samia Miled; Caryn E Outten; Jakob R Winther; Gael Palais; Benoit D'Autréaux; Agnès Delaunay-Moisan; Michel B Toledano
Journal:  Mol Cell       Date:  2017-09-14       Impact factor: 17.970

4.  Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.

Authors:  Arati Tripathi; Elisabet C Mandon; Reid Gilmore; Tom A Rapoport
Journal:  J Biol Chem       Date:  2017-03-12       Impact factor: 5.157

5.  The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.

Authors:  Christopher M Witham; Hasindu G Dassanayake; Aleshanee L Paxman; Kofi L P Stevens; Lamprini Baklous; Paris F White; Amy L Black; Robert F L Steuart; Colin J Stirling; Benjamin L Schulz; Carl J Mousley
Journal:  J Biol Chem       Date:  2019-12-17       Impact factor: 5.157

6.  Post-translational processing and membrane translocation of the yeast regulatory Mid1 subunit of the Cch1/VGCC/NALCN cation channel family.

Authors:  Kazuko Iida; Jinfeng Teng; Toshihiko Cho; Sato Yoshikawa-Kimura; Hidetoshi Iida
Journal:  J Biol Chem       Date:  2017-10-17       Impact factor: 5.157

7.  Structure of the posttranslational Sec protein-translocation channel complex from yeast.

Authors:  Samuel Itskanov; Eunyong Park
Journal:  Science       Date:  2018-12-13       Impact factor: 47.728

Review 8.  Protein-folding homeostasis in the endoplasmic reticulum and nutritional regulation.

Authors:  David Ron; Heather P Harding
Journal:  Cold Spring Harb Perspect Biol       Date:  2012-12-01       Impact factor: 10.005

9.  The SND proteins constitute an alternative targeting route to the endoplasmic reticulum.

Authors:  Naama Aviram; Tslil Ast; Elizabeth A Costa; Eric C Arakel; Silvia G Chuartzman; Calvin H Jan; Sarah Haßdenteufel; Johanna Dudek; Martin Jung; Stefan Schorr; Richard Zimmermann; Blanche Schwappach; Jonathan S Weissman; Maya Schuldiner
Journal:  Nature       Date:  2016-11-30       Impact factor: 49.962

Review 10.  Revealing functional insights into ER proteostasis through proteomics and interactomics.

Authors:  Madison T Wright; Lars Plate
Journal:  Exp Cell Res       Date:  2020-12-08       Impact factor: 3.905

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