| Literature DB >> 29187595 |
Paolo Grumati1, Ivan Dikic2,3.
Abstract
Ubiquitination is a widespread post-translational modification that controls multiple steps in autophagy, a major lysosome-mediated intracellular degradation pathway. A variety of ubiquitin chains are attached as selective labels on protein aggregates and dysfunctional organelles, thus promoting their autophagy-dependent degradation. Moreover, ubiquitin modification of autophagy regulatory components is essential to positively or negatively regulate autophagy flux in both non-selective and selective pathways. We review the current findings that elucidate the components, timing, and kinetics of the multivalent role of ubiquitin signals in control of amplitude and selectivity of autophagy pathways as well as their impact on the development of human diseases.Entities:
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Year: 2017 PMID: 29187595 PMCID: PMC5900779 DOI: 10.1074/jbc.TM117.000117
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157