Microtubule Simulations Provide Insight into the Molecular Mechanism Underlying Dynamic Instability
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1Department of Chemistry, Chicago Center for Theoretical Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois.
Abstract:
The dynamic instability of microtubules (MTs), which refers to their ability to switch between polymerization and depolymerization states, is crucial for their function. It has been proposed that the growing MT ends are protected by a "GTP cap" that consists of GTP-bound tubulin dimers. When the speed of GTP hydrolysis is faster than dimer recruitment, the loss of this GTP cap will lead the MT to undergo rapid disassembly. However, the underlying atomistic mechanistic details of the dynamic instability remains unclear. In this study, we have performed long-time atomistic molecular dynamics simulations (1 μs for each system) for MT patches as well as a short segment of a closed MT in both GTP- and GDP-bound states. Our results confirmed that MTs in the GDP state generally have weaker lateral interactions between neighboring protofilaments (PFs) and less cooperative outward bending conformational change, where the difference between bending angles of neighboring PFs tends to be larger compared with GTP ones. As a result, when the GDP state tubulin dimer is exposed at the growing MT end, these factors will be more likely to cause the MT to undergo rapid disassembly. We also compared simulation results between the special MT seam region and the remaining material and found that the lateral interactions between MT PFs at the seam region were comparatively much weaker. This finding is consistent with the experimental suggestion that the seam region tends to separate during the disassembly process of an MT.
Insights
Microtubules (MTs) switch between growth and shrinkage due to dynamic instability. GDP-bound tubulin weakens MTs, promoting disassembly, especially at the seam region, atomistic simulations reveal.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Microtubule (MT) dynamic instability is essential for cellular functions.
- Growing MT ends are protected by GTP-bound tubulin dimers, forming a GTP cap.
- Loss of the GTP cap triggers rapid MT disassembly, but atomistic mechanisms are unclear.
Purpose of the Study:
- To elucidate the atomistic mechanistic details of microtubule dynamic instability.
- To investigate the role of GTP- and GDP-bound tubulin states in MT stability.
Main Methods:
- Performed long-time (1 μs) atomistic molecular dynamics simulations.
- Simulated MT patches and a short segment of a closed MT in both GTP- and GDP-bound states.
- Compared simulation results between the MT seam region and other regions.
Main Results:
- MTs in the GDP state exhibit weaker lateral protofilament interactions and less cooperative bending compared to GTP-MTs.
- GDP-bound tubulin exposure at the MT end promotes disassembly.
- The MT seam region shows significantly weaker lateral interactions than other regions.
Conclusions:
- Weaker lateral interactions and conformational changes in GDP-MTs contribute to their disassembly.
- The MT seam region's inherent weakness facilitates its separation during disassembly.
- These findings provide atomistic insights into microtubule dynamic instability.
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