ArticleMolecular and cellular biology2005
The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
51 citing papers in PubMed, 101 citations in OpenAlex.
- Domains in Action: Understanding Ddi1's Diverse Functions in the Ubiquitin-Proteasome System.International journal of molecular sciences · 2024Review
- Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Targeting Proteasomes and the MHC Class I Antigen Presentation Machinery to Treat Cancer, Infections and Age-Related Diseases.Cancers · 2023Review
- Regulation and Functions of the ER-Associated Nrf1 Transcription Factor.Cold Spring Harbor perspectives in biology · 2023Review
- Mammalian Ddi2 is a shuttling factor containing a retroviral protease domain that influences binding of ubiquitylated proteins and proteasomal degradation.The Journal of biological chemistry · 2022Article
- Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Yeast Rpn4 Links the Proteasome and DNA Repair viaInternational journal of molecular sciences · 2020Article
- DDI2 Is a Ubiquitin-Directed Endoprotease Responsible for Cleavage of Transcription Factor NRF1.Molecular cell · 2020Article
- Multi-Step Ubiquitin Decoding Mechanism for Proteasomal Degradation.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Ddi1 is a ubiquitin-dependent protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Detailed Dissection of UBE3A-Mediated DDI1 Ubiquitination.Frontiers in physiology · 2019Article
- Inhibition of calpain-1 stabilizes TCF11/Nrf1 but does not affect its activation in response to proteasome inhibition.Bioscience reports · 2018Article
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
- Transcriptional regulation of the 26S proteasome by Nrf1.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018Review
- Comprehensive profiling of lysine ubiquitome reveals diverse functions of lysine ubiquitination in common wheat.Scientific reports · 2017Article
- Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family.Scientific reports · 2016Article
- Catalytically Active Proteasomes Function Predominantly in the Cytosol.The Journal of biological chemistry · 2016Article
- Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic protease DDI-1.eLife · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ho endonuclease initiates a mating type switch by making a double-strand break at the mating type locus, MAT. Ho is marked by phosphorylation for rapid destruction by functions of the DNA damage response, MEC1, RAD9, and CHK1. Phosphorylated Ho is recruited for ubiquitylation via the SCF ubiquitin ligase complex by the F-box protein, Ufo1. Here we identify a further DNA damage-inducible protein, the UbL-UbA protein Ddi1, specifically required for Ho degradation. Ho interacts only with Ddi1; it does not interact with the other UbL-UbA proteins, Rad23 or Dsk2. Ho must be ubiquitylated to interact with Ddi1, and there is no interaction when Ho is produced in mec1 or Deltaufo1 mutants that do not support its degradation. Ddi1 binds the proteasome via its N-terminal ubiquitin-like domain (UbL) and interacts with ubiquitylated Ho via its ubiquitin-associated domain (UbA); both domains of Ddi1 are required for association of ubiquitylated Ho with the proteasome. Despite being a nuclear protein, Ho is exported to the cytoplasm for degradation. In the absence of Ddi1, ubiquitylated Ho is stabilized and accumulates in the cytoplasm. These results establish a role for Ddi1 in the degradation of a natural ubiquitylated substrate. The specific interaction between Ho and Ddi1 identifies an additional function associated with DNA damage involved in its degradation.
Indexed as
Identifiers
What OpenQuestion holds
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.