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Front Cover: The Disordered Landscape of the 20S Proteasome Substrates Reveals Tight Association with Phase Separated Granules
Author(s) -
Myers Nadav,
Olender Tsviya,
Savidor Alon,
Levin Yishai,
Reuven Nina,
Shaul Yosef
Publication year - 2018
Publication title -
proteomics
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201870191
Subject(s) - intrinsically disordered proteins , proteasome , rna , rna binding protein , chemistry , biology , front cover , plasma protein binding , microbiology and biotechnology , computational biology , biophysics , biochemistry , cover (algebra) , gene , mechanical engineering , engineering
DOI: 10.1002/pmic.201800076 In article number 1800076 , Myers et al. report that many proteins can be degraded by the 20S Proteasome complex. RNA binding intrinsically disordered proteins (IDPs), which form phase–separated granules within the cell, are a large subset of these substrates. These proteins in addition to harboring an RNA binding domain (RBD) are enriched with prion like domains (PrLD) and low complexity domains (LCD) revealing a novel link between phase separation and 20S degradation. A small group of these proteins which are implicated in ALS disease are the most preferential 20S substrates.