ArticleNature structural & molecular biology2017
Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution.
Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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.
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.
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Who cites it
53 citing papers in PubMed, 82 citations in OpenAlex.
- Substrate recognition by human separase.Science advances · 2025Article
- Why is your separase such a big protease?Science advances · 2025Review
- Regulatory mechanisms of PP2A complex assembly driven by physicochemical differences in A-subunit isoforms.Structure (London, England : 1993) · 2025Article
- Mechanism of nascent chain removal by the ribosome-associated quality control complex.Nature communications · 2025Article
- Bacterial transcriptional repressor NrdR - a flexible multifactorial nucleotide sensor.The FEBS journal · 2025Article
- Structural mechanism of LINE-1 target-primed reverse transcription.Science (New York, N.Y.) · 2025Article
- SGO2 does not play an essential role in separase inhibition during meiosis I in mouse oocytes.PLoS biology · 2025Article
- Securin regulates the spatiotemporal dynamics of separase.The Journal of cell biology · 2025Article
- Emerging Roles of PTTG1/Securin in Breast Cancer.Journal of Cancer · 2025Review
- Structural basis for regulation of a CBASS-CRISPR-Cas defense island by a transmembrane anti-σ factor and its ECF σ partner.Science advances · 2024Article
- Article
- Securin Regulates the Spatiotemporal Dynamics of Separase.bioRxiv : the preprint server for biology · 2023Article
- The molecular mechanisms of human separase regulation.Biochemical Society transactions · 2023Review
- Separase and Roads to Disengage Sister Chromatids during Anaphase.International journal of molecular sciences · 2023Review
- Small molecule inhibitors of 15-PGDH exploit a physiologic induced-fit closing system.Nature communications · 2023Article
- Cohesin organization, dynamics, and subdomain functions revealed by genetic suppressor screening.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023Article
- Structural basis for the non-self RNA-activated protease activity of the type III-E CRISPR nuclease-protease Craspase.Nature communications · 2022Article
- Mapping separase-mediated cleavage in situ.NAR genomics and bioinformatics · 2022Article
- RNA-activated protein cleavage with a CRISPR-associated endopeptidase.Science (New York, N.Y.) · 2022Article
- Craspase is a CRISPR RNA-guided, RNA-activated protease.Science (New York, N.Y.) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Separase is a caspase-family protease that initiates chromatid segregation by cleaving the kleisin subunits (Scc1 and Rec8) of cohesin, and regulates centrosome duplication and mitotic spindle function through cleavage of kendrin and Slk19. To understand the mechanisms of securin regulation of separase, we used single-particle cryo-electron microscopy (cryo-EM) to determine a near-atomic-resolution structure of the Caenorhabditis elegans separase-securin complex. Separase adopts a triangular-shaped bilobal architecture comprising an N-terminal tetratricopeptide repeat (TPR)-like α-solenoid domain docked onto the conserved C-terminal protease domain. Securin engages separase in an extended antiparallel conformation, interacting with both lobes. It inhibits separase by interacting with the catalytic site through a pseudosubstrate mechanism, thus revealing that in the inhibited separase-securin complex, the catalytic site adopts a conformation compatible with substrate binding. Securin is protected from cleavage because an aliphatic side chain at the P1 position represses protease activity by disrupting the organization of catalytic site residues.
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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.