ArticleMolecular and cellular biology2013
Critical differences between isoforms of securin reveal mechanisms of separase regulation.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Exploring the Blood Biomarkers and Potential Therapeutic Agents for Human Acute Mountain Sickness Based on Transcriptomic Analysis, Inflammatory Infiltrates and Molecular Docking.International journal of molecular sciences · 2024Article
- SPTBN1 Mediates the Cytoplasmic Constraint of PTTG1, Impairing Its Oncogenic Activity in Human Seminoma.International journal of molecular sciences · 2023Article
- DNA damage checkpoint execution and the rules of its disengagement.Frontiers in cell and developmental biology · 2022Review
- Complex Analysis of Retroposed Genes' Contribution to Human Genome, Proteome and Transcriptome.Genes · 2020Article
- Prognostic implications of securin expression and sub-cellular localization in human breast cancer.Cellular oncology (Dordrecht, Netherlands) · 2016Article
- Structural Insights into Separase Architecture and Substrate Recognition through Computational Modelling of Caspase-Like and Death Domains.PLoS computational biology · 2015Article
- Pituitary tumor transforming gene PTTG2 induces psoriasis by regulating vimentin and E-cadherin expression.International journal of clinical and experimental pathology · 2015Article
- SGO1C is a non-functional isoform of Shugoshin and can disrupt sister chromatid cohesion by interacting with PP2A-B56.Cell cycle (Georgetown, Tex.) · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sister chromatid separation depends on the activity of separase, which in turn requires the proteolysis of its inhibitor, securin. It has been speculated that securin also supports the activation of separase. In this study, we found that PTTG1 was the major securin isoform expressed in most normal and cancer cell lines. Remarkably, a highly homologous isoform called PTTG2 was unable to interact with separase. Using chimeras between PTTG1 and PTTG2 and other approaches, we pinpointed a single amino acid that accounted for the loss of securin function in PTTG2. Mutation of the homologous position in PTTG1 (H(134)) switched PTTG1 from an inhibitor into an activator of separase. In agreement with this, PTTG1 lacking H(134) was able to trigger premature sister chromatid separation. Conversely, introduction of H(134) into PTTG2 is sufficient to allow it to bind separase. These data demonstrate that while the motif containing H(134) has a strong affinity for separase and is involved in inhibiting it, another domain(s) is involved in activating separase and has a weaker affinity for it. Although PTTG2 lacks securin function, its differences from PTTG1 provide evidence of independent inhibitory and activating functions of PTTG1 on separase.
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