A Mechanistic Model of the Actin Cycle
Biophysical Journal, 2004
| Main Authors: | , , , |
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| Format: | Article |
| Language: | en_US |
| Published: |
Biophysical Society
2005
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| Subjects: | |
| Online Access: | http://hdl.handle.net/1721.1/26696 |
| _version_ | 1811072104906358784 |
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| author | Bindschadler, M. Osborn, E. A. Dewey, C. F. Jr McGrath, J. L. |
| author_facet | Bindschadler, M. Osborn, E. A. Dewey, C. F. Jr McGrath, J. L. |
| author_sort | Bindschadler, M. |
| collection | MIT |
| description | Biophysical Journal, 2004 |
| first_indexed | 2024-09-23T09:00:57Z |
| format | Article |
| id | mit-1721.1/26696 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T09:00:57Z |
| publishDate | 2005 |
| publisher | Biophysical Society |
| record_format | dspace |
| spelling | mit-1721.1/266962019-04-10T20:14:42Z A Mechanistic Model of the Actin Cycle Bindschadler, M. Osborn, E. A. Dewey, C. F. Jr McGrath, J. L. Actin Cycle nucleotide profile actin filament Biophysical Journal, 2004 We have derived a broad, deterministic model of the steady-state actin cycle that includes its major regulatory mechanisms. Ours is the first model to solve the complete nucleotide profile within filaments, a feature that determines the dynamics and geometry of actin networks at the leading edges of motile cells, and one that has challenged investigators developing models to interpret steady-state experiments. We arrived at the nucleotide profile through analytic and numerical approaches that completely agree. Our model reproduces behaviors seen in numerous experiments with purified proteins, but allows a detailed inspection of the concentrations and fluxes that might exist in these experiments. These inspections provide new insight into the mechanisms that determine the rate of actin filament treadmilling. Specifically, we find that mechanisms for enhancing Pi release from the ADP-Pi intermediate on filaments, for increasing the off rate of ADP-bound subunits at pointed ends, and the multiple, simultaneous functions of profilin, make unique and essential contributions to increased treadmilling. In combination, these mechanisms have a theoretical capacity to increase treadmilling to levels limited only by the amount of available actin. This limitation arises because as the cycle becomes more dynamic, it tends toward the unpolymerized state. 2005-09-01T12:00:00Z 2005-09-01T12:00:00Z 2004-05 Article http://hdl.handle.net/1721.1/26696 Biophysical Journal, 86, p. 2720-2739, (2004) en_US 364500 bytes application/pdf application/pdf Biophysical Society |
| spellingShingle | Actin Cycle nucleotide profile actin filament Bindschadler, M. Osborn, E. A. Dewey, C. F. Jr McGrath, J. L. A Mechanistic Model of the Actin Cycle |
| title | A Mechanistic Model of the Actin Cycle |
| title_full | A Mechanistic Model of the Actin Cycle |
| title_fullStr | A Mechanistic Model of the Actin Cycle |
| title_full_unstemmed | A Mechanistic Model of the Actin Cycle |
| title_short | A Mechanistic Model of the Actin Cycle |
| title_sort | mechanistic model of the actin cycle |
| topic | Actin Cycle nucleotide profile actin filament |
| url | http://hdl.handle.net/1721.1/26696 |
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