Open AccessCellular proteostasis: degradation of misfolded proteins by lysosomes
Author(s) -
Matthew P. Jackson,
Eric W. Hewitt
Publication year - 2016
Publication title -
essays in biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.351
H-Index - 66
eISSN - 1744-1358
pISSN - 0071-1365
DOI - 10.1042/ebc20160005
Subject(s) - proteostasis , autophagy , microbiology and biotechnology , amyloid disease , protein folding , biogenesis , biology , protein aggregation , lysosome , aggresome , endocytosis , tfeb , proteolysis , protein degradation , endoplasmic reticulum associated protein degradation , chaperone (clinical) , biochemistry , unfolded protein response , endoplasmic reticulum , amyloid fibril , amyloid β , cell , enzyme , medicine , apoptosis , disease , pathology , gene
Proteostasis refers to the regulation of the cellular concentration, folding, interactions and localization of each of the proteins that comprise the proteome. One essential element of proteostasis is the disposal of misfolded proteins by the cellular pathways of protein degradation. Lysosomes are an important site for the degradation of misfolded proteins, which are trafficked to this organelle by the pathways of macroautophagy, chaperone-mediated autophagy and endocytosis. Conversely, amyloid diseases represent a failure in proteostasis, in which proteins misfold, forming amyloid deposits that are not degraded effectively by cells. Amyloid may then exacerbate this failure by disrupting autophagy and lysosomal proteolysis. However, targeting the pathways that regulate autophagy and the biogenesis of lysosomes may present approaches that can rescue cells from the deleterious effects of amyloidogenic proteins.
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