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New MAPS for misfolded proteins
Clearing misfolded proteins from the cytoplasm is essential to maintain cellular homeostasis. Now, a parallel clearance system is described that uses the deubiquitylase USP19 to enable secretion of misfolded cytoplasmic proteins when conventional proteasomal degradation is compromised. Misfolding-associated protein secretion (MAPS) has important implications for protein quality control and prion-like transmission.
- Norbert Volkmar
- , Emma Fenech
- & John C. Christianson
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Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells
Lee et al. report that aberrantly folded cytosolic proteins are recruited to the ER by the USP19 deubiquitylase, and are then encapsulated in late endosomes that fuse with the plasma membrane, leading to their secretion.
- Jin-Gu Lee
- , Shokichi Takahama
- & Yihong Ye
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Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane
How misfolded proteins are extracted from the endoplasmic reticulum (ER) for degradation remains unclear. Sommer and colleagues demonstrate that following assembly into the HRD ligase complex, Der1 forms oligomers in the ER membrane and enables extraction of proteins from the ER lumen.
- Martin Mehnert
- , Thomas Sommer
- & Ernst Jarosch
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Defining human ERAD networks through an integrative mapping strategy
Improperly folded proteins are targeted for destruction through the endoplasmic-reticulum-associated degradation pathway (ERAD). Kopito and colleagues present a high-resolution interaction analysis of the ERAD system in combination with functional genomics, and identify new ERAD components.
- John C. Christianson
- , James A. Olzmann
- & Ron R. Kopito
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BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol
Non-enveloped viruses such as SV40 are transported from the extracellular space into the host cell nucleus through a pathway involving endocytosis, trafficking to the endoplasmic reticulum (ER) lumen, transport across the ER membrane to the cytoplasm, and subsequent nuclear import. Helenius and colleagues provide insight into how SV40 escapes from the ER by showing that viral proteins interact with components of the host ER-associated degradation machinery (ERAD). These interactions are crucial for translocation of SV40 into the cytoplasm and infectivity.
- Roger Geiger
- , Daniel Andritschke
- & Ari Helenius
ER-associated RNA silencing promotes ER quality control