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Separase anxiety: dissolving the sister bond and more
1Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA. david_pellman@dfci.harvard.edu
Nature Cell Biology
|September 5, 2001
Summary
Separase, a key enzyme in cell division, may have more destructive functions than previously believed. New research suggests separase shares destructive impulses with caspases, its relatives.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Separase is a protease essential for cell division.
- It functions by cleaving sister chromatid cohesion.
- Previously, separase was considered a highly regulated protease with limited substrates.
Purpose of the Study:
- To investigate the substrate specificity and regulation of separase.
- To explore potential novel functions of separase beyond sister chromatid separation.
- To compare the functional characteristics of separase with its relatives, caspases.
Main Methods:
- Biochemical assays to assess separase protease activity.
- Mass spectrometry to identify separase substrates.
- Cellular imaging to observe separase function in vivo.
Main Results:
- New findings indicate separase may cleave more substrates than previously known.
- Evidence suggests separase possesses 'atavistic impulses', similar to caspases.
- This implies a broader and potentially more destructive role for separase.
Conclusions:
- Separase's function may be more complex and less repressed than previously understood.
- The enzyme shares functional similarities with caspases, suggesting conserved destructive mechanisms.
- Further research is needed to fully elucidate separase's expanded role in cellular processes.
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