| Title: |
A global, myosin light chain kinase-dependent increase in myosin II contractility accompanies the metaphase–anaphase transition in sea urchin eggs |
| Authors: |
Lucero, Amy; Stack, Christianna; Bresnick, Anne R.; Shuster, Charles B. |
| Source: |
Molecular Biology of the Cell 17 (2006): 4093-4104 ; doi:10.1091/mbc.E06-02-0119 |
| Publisher Information: |
American Society for Cell Biology |
| Publication Year: |
2006 |
| Collection: |
Woods Hole Scientific Community: WHOAS (Woods Hole Open Access Server) |
| Description: |
Author Posting. © American Society for Cell Biology, 2006. This article is posted here by permission of American Society for Cell Biology for personal use, not for redistribution. The definitive version was published in Molecular Biology of the Cell 17 (2006): 4093-4104, doi:10.1091/mbc.E06-02-0119. ; Myosin II is the force-generating motor for cytokinesis, and although it is accepted that myosin contractility is greatest at the cell equator, the temporal and spatial cues that direct equatorial contractility are not known. Dividing sea urchin eggs were placed under compression to study myosin II-based contractile dynamics, and cells manipulated in this manner underwent an abrupt, global increase in cortical contractility concomitant with the metaphase–anaphase transition, followed by a brief relaxation and the onset of furrowing. Prefurrow cortical contractility both preceded and was independent of astral microtubule elongation, suggesting that the initial activation of myosin II preceded cleavage plane specification. The initial rise in contractility required myosin light chain kinase but not Rho-kinase, but both signaling pathways were required for successful cytokinesis. Last, mobilization of intracellular calcium during metaphase induced a contractile response, suggesting that calcium transients may be partially responsible for the timing of this initial contractile event. Together, these findings suggest that myosin II-based contractility is initiated at the metaphase–anaphase transition by Ca2+-dependent myosin light chain kinase (MLCK) activity and is maintained through cytokinesis by both MLCK- and Rho-dependent signaling. Moreover, the signals that initiate myosin II contractility respond to specific cell cycle transitions independently of the microtubule-dependent cleavage stimulus. ; This work was supported by grants from the National Institute of General Medical Sciences (GM08136 and GM61222), and the Robert Day Allen and Baxter fellowships at the Marine Biological Laboratory. |
| Document Type: |
article in journal/newspaper |
| File Description: |
video/quicktime; application/pdf |
| Language: |
English |
| Relation: |
https://doi.org/10.1091/mbc.E06-02-0119; Molecular Biology of the Cell 17 (2006): 4093-4104; https://hdl.handle.net/1912/1843 |
| Availability: |
https://hdl.handle.net/1912/1843 |
| Accession Number: |
edsbas.328834C7 |
| Database: |
BASE |