Cited by 222Microtubule and mitosis dynamicsDNA Repair MechanismsUbiquitin and proteasome pathways

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Regulation of Human Separase by Securin Binding and Autocleavage

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Waizenegger, Irene C., Giménez-Abián, Juan F., Wernic, Dominik, Peters, Jan-Michael·2002·Current Biology

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Abstract

Background Sister chromatid separation is initiated by separase, a protease that cleaves cohesin and thereby dissolves sister chromatid cohesion. Separase is activated by the degradation of its inhibitor securin and by the removal of inhibitory phosphates. In human cells, separase activation also coincides with the cleavage of separase, but it is not known if this reaction activates separase, which protease cleaves separase, and how separase cleavage is regulated. Results Inhibition of separase expression in human cells by RNA interference causes the formation of polyploid cells with large lobed nuclei. In mitosis, many of these cells contain abnormal chromosome plates with unseparated sister chromatids. Inhibitor binding experiments in vitro reveal that securin prevents the access of substrate analogs to the active site of separase. Upon securin degradation, the active site of full-length separase becomes accessible, allowing rapid autocatalytic cleavage of separase at one of three sites. The resulting N- and C-terminal fragments remain associated and can be reinhibited by securin. A noncleavable separase mutant retains its ability to cleave cohesin in vitro. Conclusions Our results suggest that separase is required for sister chromatid separation during mitosis in human cells. Our data further indicate that securin inhibits separase by blocking the access of substrates to the active site of separase. Securin proteolysis allows autocatalytic processing of separase into a cleaved form, but separase cleavage is not essential for separase activation.

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Authors: Waizenegger, I. C., Giménez-Abián, J. F., Wernic, D., & Peters, J.-M.
Affiliations: Research Institute of Molecular Pathology (AT)
Consejo Superior de Investigaciones Científicas (ES)
Boehringer Ingelheim (Canada) (CA)
Corresponding author: Peters, Jan-Michael
ORCID: Waizenegger, Irene C.
Giménez-Abián, Juan F.
Wernic, Dominik
Peters, Jan-Michael
Venue: Current Biology
Publisher: Elsevier BV
Published: 2002-08
Volume: 12
Issue: 16
Pages: 1368-1378
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/s0960-9822(02)01073-4
OpenAlex: W1967853904
Cited by: 222
References: 40
Citations by year: 2026: 7 · 2025: 11 · 2024: 7 · 2023: 8 · 2022: 9 · 2021: 5 · 2020: 8 · 2019: 10 · 2018: 7 · 2017: 15 · 2016: 10 · 2015: 8 · 2014: 6 · 2013: 7 · 2012: 9
FWCI: 3.89
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4003 d)
Locations: Current Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: separase, securin, sister chromatid separation, cohesin cleavage, sister chromatid cohesion, autocatalytic cleavage, protease activation, mitosis, polyploidy, active site inhibition, RNA interference
MeSH terms: Amino Acid Sequence, Animals, Cell Nucleus, Chromosomal Proteins, Non-Histone, Chromosomes, Enzyme Activation, Enzyme Inhibitors, Fungal Proteins, HeLa Cells, Humans, Mitosis, Models, Biological, Neoplasm Proteins, Nuclear Proteins, Endopeptidases, Peptides, Phosphoproteins, Polyploidy, Protein Binding, Molecular Structure, Trans-Activators, Sequence Alignment, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins, RNA Interference, Separase, Securin

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Regulation of Human Separase by Securin Binding and Autocleavage

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