Premium
Fighting disease by selective autophagy of aggregate‐prone proteins
Author(s) -
Knævelsrud Helene,
Simonsen Anne
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.041
Subject(s) - autophagy , ubiquitin , microbiology and biotechnology , protein aggregation , proteasome , organelle , protein degradation , biology , receptor , bag3 , lysosome , chemistry , biochemistry , enzyme , apoptosis , gene
Ubiquitinated protein aggregates are hallmarks of a range of human diseases, including neurodegenerative, liver and muscle disorders. These protein aggregates are typically positive for the autophagy receptor p62. Whereas the ubiquitin‐proteasome system (UPS) degrades shortlived and misfolded ubiquitinated proteins that are small enough to enter the narrow pore of the barrel‐shaped proteasome, the lysosomal pathway of autophagy can degrade larger structures including entire organelles or protein aggregates. This degradation requires autophagy receptors that link the cargo with the molecular machinery of autophagy and is enhanced by certain posttranslational modifications of the cargo. In this review we focus on how autophagy clears aggregate‐prone proteins and the relevance of this process to protein aggregate associated diseases.