Derlins with scissors: primordial ERAD in bacteria

Rhomboid intramembrane serine proteases are present in all kingdoms of life, but as we do not know their substrates in many species, it remains puzzling why rhomboids are among the most‐conserved integral membrane proteins. Two new studies in The EMBO Journal by Began et al and Liu et al now link ba...

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Bibliographic Details
Published in:The EMBO journal 2020-05, Vol.39 (10), p.e105012-n/a
Main Authors: Knopf, Julia D, Lemberg, Marius K
Format: Article
Language:English
Subjects:
ATPases Associated with Diverse Cellular Activities
Bacteria - metabolism
Bacterial Proteins - metabolism
Biodegradation
Cutting tools
EMBO20
EMBO31
EMBO32
Endoplasmic Reticulum-Associated Degradation
Licensure
Membrane proteins
Membrane Proteins - metabolism
Membranes
Membranes - metabolism
News & Views
Peptide Hydrolases - metabolism
Proteins
Rhomboids
Serine
Substrates
Views
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Summary:Rhomboid intramembrane serine proteases are present in all kingdoms of life, but as we do not know their substrates in many species, it remains puzzling why rhomboids are among the most‐conserved integral membrane proteins. Two new studies in The EMBO Journal by Began et al and Liu et al now link bacterial rhomboid proteases to membrane protein degradation, showing striking similarities to what is known about eukaryotic rhomboid family proteins, thus pointing toward a conserved membrane surveillance mechanism. Graphical Abstract Recent studies describing new rhomboid protease substrates and roles reveal striking functional analogies between eukaryotic and prokaryotic family members.
ISSN:0261-4189
1460-2075
DOI:10.15252/embj.2020105012