Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 18, Issue 12, Pages 5081-5090Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E06-12-1076
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Funding
- NHLBI NIH HHS [HL073050, R01 HL073050] Funding Source: Medline
- NIAMS NIH HHS [R01 AR048898, R01 AR041653, AR048898, AR41653, R01 AR048526, AR048526] Funding Source: Medline
- NIDCD NIH HHS [DC006103, R01 DC006103] Funding Source: Medline
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Phosphorylation of the regulatory light chain of myosin II (MLC20) at the activation sites promotes both the motor activity and the filament formation of myosin II, thus playing an important role in various cell motile processes. In contrast, the physiological function of phosphorylation of MLC20 at the inhibitory sites is unknown. Here we report for the first time the function of the inhibitory site phosphorylation in the cells. We successfully produced the antibodies specifically recognizing the phosphorylation sites of MLC20 at Ser1, and the platelet-derived growth factor (PDGF)-induced change in the phosphorylation at the Ser1 was monitored. The phosphorylation of MLC20 at the Ser1 significantly increased during the PDGF-induced actin cytoskeletal reorganization. PDGF disassembled the stress fibers, and this was attenuated with the expression of unphosphorylatable MLC20 at the Ser1/Ser2 phosphorylation sites. The present results suggest that the down-regulation of myosin II activity achieved by the phosphorylation at the Ser1/Ser2 sites plays an important role in the normal reorganization of actomyosin filaments triggered by PDGF receptor stimulation.
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