ArticleMolecular biology of the cell2010
Proteasome nuclear import mediated by Arc3 can influence efficient DNA damage repair and mitosis in Schizosaccharomyces pombe.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
- Induction of N-Ras degradation by flunarizine-mediated autophagy.Scientific reports · 2018Article
- Stress induced nuclear granules form in response to accumulation of misfolded proteins in Caenorhabditis elegans.BMC cell biology · 2017Article
- UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.Cell stress & chaperones · 2017Article
- Calcification of primary human osteoblast cultures under flow conditions using polycaprolactone scaffolds for intravascular applications.Journal of tissue engineering and regenerative medicine · 2012Article
- Involvement of the nuclear proteasome activator PA28γ in the cellular response to DNA double-strand breaks.Cell cycle (Georgetown, Tex.) · 2011Article
- Schizosaccharomyces pombe Arc3 is a conserved subunit of the Arp2/3 complex required for polarity, actin organization, and endocytosis.Yeast (Chichester, England) · 2011Article
- Nuclear import of an intact preassembled proteasome particle.Molecular biology of the cell · 2011Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Proteasomes must remove regulatory molecules and abnormal proteins throughout the cell, but how proteasomes can do so efficiently remains unclear. We have isolated a subunit of the Arp2/3 complex, Arc3, which binds proteasomes. When overexpressed, Arc3 rescues phenotypes associated with proteasome deficiencies; when its expression is repressed, proteasome deficiencies intensify. Arp2/3 is best known for regulating membrane dynamics and vesicular transport; thus, we performed photobleaching experiments and showed that proteasomes are readily imported into the nucleus but exit the nucleus slowly. Proteasome nuclear import is reduced when Arc3 is inactivated, leading to hypersensitivity to DNA damage and inefficient cyclin-B degradation, two events occurring in the nucleus. These data suggest that proteasomes display Arc3-dependent mobility in the cell, and mobile proteasomes can efficiently access substrates throughout the cell, allowing them to effectively regulate cell-compartment-specific activities.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.