Literature DB >> 18680510

Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.

Chantal Christis1, Nicolette H Lubsen, Ineke Braakman.   

Abstract

A correct three-dimensional structure is a prerequisite for protein functionality, and therefore for life. Thus, it is not surprising that our cells are packed with proteins that assist protein folding, the process in which the native three-dimensional structure is formed. In general, plasma membrane and secreted proteins, as well as those residing in compartments along the endocytic and exocytic pathways, fold and oligomerize in the endoplasmic reticulum. The proteins residing in the endoplasmic reticulum are specialized in the folding of this subset of proteins, which renders this compartment a protein-folding factory. This review focuses on protein folding in the endoplasmic reticulum, and discusses the challenge of oligomer formation in the endoplasmic reticulum as well as the cytosol.

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Year:  2008        PMID: 18680510     DOI: 10.1111/j.1742-4658.2008.06590.x

Source DB:  PubMed          Journal:  FEBS J        ISSN: 1742-464X            Impact factor:   5.542


  25 in total

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5.  Regulated increase in folding capacity prevents unfolded protein stress in the ER.

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