Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.cell.2008.09.018
Title: A Tripartite Complex Containing MRCK Modulates Lamellar Actomyosin Retrograde Flow
Authors: Tan, I.
Yong, J.
Dong, J.M.
Lim, L.
Leung, T. 
Keywords: CELLBIO
Issue Date: 3-Oct-2008
Citation: Tan, I., Yong, J., Dong, J.M., Lim, L., Leung, T. (2008-10-03). A Tripartite Complex Containing MRCK Modulates Lamellar Actomyosin Retrograde Flow. Cell 135 (1) : 123-136. ScholarBank@NUS Repository. https://doi.org/10.1016/j.cell.2008.09.018
Abstract: Actomyosin retrograde flow underlies the contraction essential for cell motility. Retrograde flow in both lamellipodia and lamella is required for membrane protrusion and for force generation by coupling to cell adhesion. We report that the Rac/Cdc42-binding kinase MRCK and myosin II-related MYO18A linked by the adaptor protein LRAP35a form a functional tripartite complex, which is responsible for the assembly of lamellar actomyosin bundles and of a subnuclear actomyosin network. LRAP35a binds independently to MYO18A and MRCK. This binding leads to MRCK activation and its phosphorylation of MYO18A, independently of ROK and MLCK. The MRCK complex moves in concert with the retrograde flow of actomyosin bundles, with MRCK being able to influence other flow components such as MYO2A. The promotion of persistent protrusive activity and inhibition of cell motility by the respective expression of wild-type and dominant-negative mutant components of the MRCK complex show it to be crucial to cell protrusion and migration. © 2008 Elsevier Inc. All rights reserved.
Source Title: Cell
URI: http://scholarbank.nus.edu.sg/handle/10635/108243
ISSN: 00928674
DOI: 10.1016/j.cell.2008.09.018
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