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The Bub2p spindle checkpoint links nuclear migration with mitotic exit.
G Pereira1, T Höfken, J Grindlay
1The Beatson Institute for Cancer Research, CRC Beatson Laboratories, Glasgow, United Kingdom.
Molecular Cell
|August 19, 2000
Summary
The budding yeast spindle pole body (SPB) proteins Bfa1p and Bub2p link nuclear migration to mitotic exit by regulating Tem1p GTPase activity. SPB positioning is proposed to control mitotic exit timing in conserved pathways.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Bfa1p and Bub2p are spindle checkpoint proteins associated with the spindle pole body (SPB).
- These proteins are thought to possess GTPase activation capabilities.
- They play a role in the budding yeast mitotic exit network.
Purpose of the Study:
- To investigate the interaction between Bfa1p, Bub2p, and Tem1p.
- To elucidate the role of SPB localization in regulating Tem1p activity.
- To understand the mechanism linking nuclear migration and mitotic exit.
Main Methods:
- Protein localization studies using budding yeast.
- Analysis of GTPase activation and binding interactions.
- Investigating the role of Lte1p in Tem1p regulation.
Main Results:
- Bfa1p and Bub2p localize Tem1p to the SPB's cytoplasmic face in the bud.
- Lte1p is found at the bud cortex, facilitating Tem1p activation.
- SPB migration into the bud is critical for Tem1p activation and mitotic exit.
Conclusions:
- SPB positioning is a key regulatory mechanism for mitotic exit in budding yeast.
- The Bfa1p-Bub2p-Tem1p pathway links nuclear migration to cell cycle progression.
- Conserved components suggest SPB/centrosome position may control mitotic exit timing across species.