Abstract
In mammalian nonmuscle cells, the mechanisms controlling the localized formation of myosin-II filaments are not well defined. To investigate the mechanisms mediating filament assembly and disassembly during generalized motility and chemotaxis, we examined the EGF-dependent phosphorylation of the myosin-IIA heavy chain in human breast cancer cells. EGF stimulation of MDA-MB-231 cells resulted in transient increases in both the assembly and phosphorylation of the myosin-IIA heavy chains. In EGF-stimulated cells, the myosin-IIA heavy chain is phosphorylated on the casein kinase 2 site (S1943). Cells expressing green fluorescent protein-myosin-IIA heavy-chain S1943E and S1943D mutants displayed increased migration into a wound and enhanced EGF-stimulated lamellipod extension compared with cells expressing wild-type myosin-IIA. In contrast, cells expressing the S1943A mutant exhibited reduced migration and lamellipod extension. These observations support a direct role for myosin-IIA heavy-chain phosphorylation in mediating motility and chemotaxis.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3144-3155 |
| Number of pages | 12 |
| Journal | Molecular Biology of the Cell |
| Volume | 18 |
| Issue number | 8 |
| DOIs | |
| State | Published - Aug 2007 |
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ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Cell Biology
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Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells. / Dulianinova, Natalia; House, Reniqua P.; Betapudi, Venkaiah; Bresnick, Anne R.
In: Molecular Biology of the Cell, Vol. 18, No. 8, 08.2007, p. 3144-3155.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells
AU - Dulianinova, Natalia
AU - House, Reniqua P.
AU - Betapudi, Venkaiah
AU - Bresnick, Anne R.
PY - 2007/8
Y1 - 2007/8
N2 - In mammalian nonmuscle cells, the mechanisms controlling the localized formation of myosin-II filaments are not well defined. To investigate the mechanisms mediating filament assembly and disassembly during generalized motility and chemotaxis, we examined the EGF-dependent phosphorylation of the myosin-IIA heavy chain in human breast cancer cells. EGF stimulation of MDA-MB-231 cells resulted in transient increases in both the assembly and phosphorylation of the myosin-IIA heavy chains. In EGF-stimulated cells, the myosin-IIA heavy chain is phosphorylated on the casein kinase 2 site (S1943). Cells expressing green fluorescent protein-myosin-IIA heavy-chain S1943E and S1943D mutants displayed increased migration into a wound and enhanced EGF-stimulated lamellipod extension compared with cells expressing wild-type myosin-IIA. In contrast, cells expressing the S1943A mutant exhibited reduced migration and lamellipod extension. These observations support a direct role for myosin-IIA heavy-chain phosphorylation in mediating motility and chemotaxis.
AB - In mammalian nonmuscle cells, the mechanisms controlling the localized formation of myosin-II filaments are not well defined. To investigate the mechanisms mediating filament assembly and disassembly during generalized motility and chemotaxis, we examined the EGF-dependent phosphorylation of the myosin-IIA heavy chain in human breast cancer cells. EGF stimulation of MDA-MB-231 cells resulted in transient increases in both the assembly and phosphorylation of the myosin-IIA heavy chains. In EGF-stimulated cells, the myosin-IIA heavy chain is phosphorylated on the casein kinase 2 site (S1943). Cells expressing green fluorescent protein-myosin-IIA heavy-chain S1943E and S1943D mutants displayed increased migration into a wound and enhanced EGF-stimulated lamellipod extension compared with cells expressing wild-type myosin-IIA. In contrast, cells expressing the S1943A mutant exhibited reduced migration and lamellipod extension. These observations support a direct role for myosin-IIA heavy-chain phosphorylation in mediating motility and chemotaxis.
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U2 - 10.1091/mbc.E06-11-1056
DO - 10.1091/mbc.E06-11-1056
M3 - Article
C2 - 17567956
AN - SCOPUS:34547757869
VL - 18
SP - 3144
EP - 3155
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 8
ER -