Literature DB >> 1772654

Degradation of proteins within the endoplasmic reticulum.

J S Bonifacino1, J Lippincott-Schwartz.   

Abstract

Certain newly synthesized proteins within the endoplasmic reticulum undergo rapid turnover by a non-lysosomal proteolytic pathway. Biochemical and morphological evidence has suggested that these proteins never leave the endoplasmic reticulum before they are degraded. The mechanism(s) for the selective targeting of proteins for degradation within the endoplasmic reticulum is still not understood, but appears to rely on specific structural determinants on the protein substrates. Important cellular functions are likely to be served by this endoplasmic reticulum degradative system, including disposal of abnormal proteins and the selective turnover of metabolically regulated proteins.

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Year:  1991        PMID: 1772654     DOI: 10.1016/0955-0674(91)90028-w

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN: 0955-0674            Impact factor:   8.382


  62 in total

1.  The principle of delivery of T cell epitopes to antigen-presenting cells applied to peptides from influenza virus, ovalbumin, and hen egg lysozyme: implications for peptide vaccination.

Authors:  I B Rasmussen; E Lunde; T E Michaelsen; B Bogen; I Sandlie
Journal:  Proc Natl Acad Sci U S A       Date:  2001-08-21       Impact factor: 11.205

Review 2.  The unfolded protein response in protein aggregating diseases.

Authors:  Alexander Gow; Ramaswamy Sharma
Journal:  Neuromolecular Med       Date:  2003       Impact factor: 3.843

Review 3.  Endoplasmic reticulum: a dynamic patchwork of specialized subregions.

Authors:  R Sitia; J Meldolesi
Journal:  Mol Biol Cell       Date:  1992-10       Impact factor: 4.138

4.  Characterization of an endoplasmic reticulum retention signal in the rubella virus E1 glycoprotein.

Authors:  T C Hobman; H F Lemon; K Jewell
Journal:  J Virol       Date:  1997-10       Impact factor: 5.103

5.  A vitellogenic-like carboxypeptidase expressed by human macrophages is localized in endoplasmic reticulum and membrane ruffles.

Authors:  James Harris; Nicole Schwinn; James A Mahoney; Hsi-Hsien Lin; Michael Shaw; Chris J Howard; Rosangela P da Silva; Siamon Gordon
Journal:  Int J Exp Pathol       Date:  2006-02       Impact factor: 1.925

6.  An engineered glutamate-gated chloride (GluCl) channel for sensitive, consistent neuronal silencing by ivermectin.

Authors:  Shawnalea J Frazier; Bruce N Cohen; Henry A Lester
Journal:  J Biol Chem       Date:  2013-05-29       Impact factor: 5.157

7.  Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.

Authors:  T Biederer; C Volkwein; T Sommer
Journal:  EMBO J       Date:  1996-05-01       Impact factor: 11.598

8.  Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein.

Authors:  T U Mayer; T Braun; S Jentsch
Journal:  EMBO J       Date:  1998-06-15       Impact factor: 11.598

9.  Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase.

Authors:  R Y Hampton; H Bhakta
Journal:  Proc Natl Acad Sci U S A       Date:  1997-11-25       Impact factor: 11.205

10.  Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole.

Authors:  J J Pueyo; M J Chrispeels; E M Herman
Journal:  Planta       Date:  1995       Impact factor: 4.116

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