Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/235481
Type: Artigo de periódico
Title: Disaggregases, Molecular Chaperones That Resolubilize Protein Aggregates.
Author: Mokry, David Z
Abrahão, Josielle
Ramos, Carlos H I
Abstract: The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance.
Citation: Anais Da Academia Brasileira De Ciências. v. 87, n. 2 Suppl, p. 1273-1292, 2015-Aug.
Rights: fechado
Identifier DOI: 10.1590/0001-3765201520140671
Address: http://www.ncbi.nlm.nih.gov/pubmed/?term=26312418
Date Issue: 2015
Appears in Collections:Unicamp - Artigos e Outros Documentos

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