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.
journal_name
Celljournal_title
Cellauthors
Tan I,Yong J,Dong JM,Lim L,Leung Tdoi
10.1016/j.cell.2008.09.018subject
Has Abstractpub_date
2008-10-03 00:00:00pages
123-36issue
1eissn
0092-8674issn
1097-4172pii
S0092-8674(08)01140-9journal_volume
135pub_type
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