ArticleNucleus (Austin, Tex.)
Sem1: a versatile "molecular glue"?
Article in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Conformational stability of PCID2 upon DSS1 binding with molecular dynamics simulation.Journal of molecular modeling · 2015Article
- Disordered proteinaceous machines.Chemical reviews · 2014Review
- The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome.Molecular biology of the cell · 2013Article
- A novel role for Sem1 and TREX-2 in transcription involves their impact on recruitment and H2B deubiquitylation activity of SAGA.Nucleic acids research · 2013Article
- Homologous recombination and its regulation.Nucleic acids research · 2012Review
- Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.Nature structural & molecular biology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The evolutionary conserved protein Sem1/Dss1 is a bona fide subunit of the regulatory particle (RP) of the proteasome and in mammalian cells stabilizes the tumor suppressor protein BRCA2. A recent study from our laboratory has revealed an unexpected non- proteasomal role of Sem1 in mRNA export. We found that Sem1, independent of the RP, is a functional component of the nuclear pore associated TREX-2 complex that is directly involved in the dynamic relocalization of a subset of DNA loci to the nuclear periphery. Like other components of TREX-2, Sem1 is required for proper nuclear export of mRNAs, transcription elongation and preventing transcription-associated genomic instability. Strikingly, Sem1 associates with a third multi-subunit protein complex namely the COP9 signalosome, which is involved in de-neddylation. We propose that Sem1 is a versatile protein that regulates the functional integrity of multiple protein complexes involved in diverse biological pathways.
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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.