Literature DB >> 16126486

Versatility of the endoplasmic reticulum protein folding factory.

Eelco van Anken1, Ineke Braakman.   

Abstract

The endoplasmic reticulum (ER) is dedicated to import, folding and assembly of all proteins that travel along or reside in the secretory pathway of eukaryotic cells. Folding in the ER is special. For instance, newly synthesized proteins are N-glycosylated and by default form disulfide bonds in the ER, but not elsewhere in the cell. In this review, we discuss which features distinguish the ER as an efficient folding factory, how the ER monitors its output and how it disposes of folding failures.

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Year:  2005        PMID: 16126486     DOI: 10.1080/10409230591008161

Source DB:  PubMed          Journal:  Crit Rev Biochem Mol Biol        ISSN: 1040-9238            Impact factor:   8.250


  81 in total

1.  ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery.

Authors:  Chunwei Walter Lai; Joel H Otero; Linda M Hendershot; Erik Snapp
Journal:  J Biol Chem       Date:  2012-01-20       Impact factor: 5.157

2.  The UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradation.

Authors:  David P LaLonde; Anthony Bretscher
Journal:  J Biol Chem       Date:  2010-12-06       Impact factor: 5.157

3.  Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells.

Authors:  Erik L Snapp; Ajay Sharma; Jennifer Lippincott-Schwartz; Ramanujan S Hegde
Journal:  Proc Natl Acad Sci U S A       Date:  2006-04-14       Impact factor: 11.205

4.  The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system.

Authors:  Sae-Hun Park; Natalia Bolender; Frederik Eisele; Zlatka Kostova; Junko Takeuchi; Philip Coffino; Dieter H Wolf
Journal:  Mol Biol Cell       Date:  2006-10-25       Impact factor: 4.138

5.  Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf.

Authors:  Shekar Menon; Jaemin Lee; William A Abplanalp; Sung-Eun Yoo; Takashi Agui; Sen-Ichi Furudate; Paul S Kim; Peter Arvan
Journal:  J Biol Chem       Date:  2007-01-02       Impact factor: 5.157

Review 6.  The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation).

Authors:  Jeffrey L Brodsky
Journal:  Biochem J       Date:  2007-06-15       Impact factor: 3.857

Review 7.  Protein energetics in maturation of the early secretory pathway.

Authors:  R Luke Wiseman; Atanas Koulov; Evan Powers; Jeffery W Kelly; William E Balch
Journal:  Curr Opin Cell Biol       Date:  2007-08-07       Impact factor: 8.382

8.  Decreased enzyme activities of chaperones PDI and BiP in aged mouse livers.

Authors:  Jonathan E Nuss; Kashyap B Choksi; James H DeFord; John Papaconstantinou
Journal:  Biochem Biophys Res Commun       Date:  2007-11-09       Impact factor: 3.575

Review 9.  Generating disulfides with the Quiescin-sulfhydryl oxidases.

Authors:  Erin J Heckler; Pumtiwitt C Rancy; Vamsi K Kodali; Colin Thorpe
Journal:  Biochim Biophys Acta       Date:  2007-10-12

10.  The unfolded protein response of B-lymphocytes: PERK-independent development of antibody-secreting cells.

Authors:  Jennifer N Gass; Hao-Yuan Jiang; Ronald C Wek; Joseph W Brewer
Journal:  Mol Immunol       Date:  2007-09-05       Impact factor: 4.407

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