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Updated: May 19, 2026

Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
Alternative nuclear transport for cellular protein quality control
April Rose1, Christian Schlieker
1Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, Bass 236A, New Haven, CT 06520-8114, USA.
Abstract:
Herpesvirus capsids traverse the nuclear envelope (NE) by utilizing an unusual export pathway termed nuclear egress. In this process, the viral capsid is delivered into the perinuclear space (PNS), producing a vesicular intermediate after fission. After fusion with the outer nuclear membrane (ONM), the naked capsid is released into the cytosol. A recent study now suggests that this pathway might be an endogenous cellular pathway, co-opted by viruses, that serves to transport cellular cargo exceeding the size limit imposed by the nuclear pore complex (NPC). We propose that one function of this pathway is to transport nuclear protein aggregates to the cytosolic autophagy machinery. Our model has implications for our understanding of laminopathies and related diseases affecting proteins residing at the inner nuclear membrane (INM) and nuclear lamina.
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