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Degradation-mediated protein quality control at the inner nuclear membrane
AuthorFoisner, Roland ; Boban, Mirta
Published in
Nucleus, Philadelphia, 2016, Vol. 7, Issue 1, page 41-49
PublishedPhiladelphia : Taylor & Francis, 2016
Document typeJournal Article
Keywords (EN)reticulum-associated degradation / ubiquitin-proteasome pathway / peroxisomal import receptor / endoplasmic-reticulum / saccharomyces-cerevisiae / intracellular-localization / transcription factors / unanswered questions / selective autophagy / mammalian-cells
Project-/ReportnumberP 23805-B20
URNurn:nbn:at:at-ubmuw:3-1414 Persistent Identifier (URN)
 The work is publicly available
Degradation-mediated protein quality control at the inner nuclear membrane [1.26 mb]
Abstract (English)

An intricate machinery protects cells from the accumulation of misfolded, non-functional proteins and protein aggregates. Protein quality control pathways have been best described in the cytoplasm and the endoplasmic reticulum, however, recent findings indicate that the nucleus is also an important compartment for protein quality control. Several nuclear ubiquitinylation pathways target soluble and membrane proteins in the nucleus and mediate their degradation through nuclear proteasomes. In addition, emerging data suggest that nuclear envelope components are also degraded by autophagy, although the mechanisms by which cytoplasmic autophagy machineries get access to nuclear targets remain unclear. In this minireview we summarize the nuclear ubiquitin-proteasome pathways in yeast, focusing on pathways involved in the protein degradation at the inner nuclear membrane. In addition, we discuss potential mechanisms how nuclear targets at the nuclear envelope may be delivered to the cytoplasmic autophagy pathways in yeast and mammals.

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