Key result
Mitosis-specific phosphorylation of the myosin phosphatase targeting subunit increased its binding to myosin II by two- to threefold and more than doubled myosin phosphatase activity.
Population
Cells (in vivo) and in vitro models studying myosin phosphatase targeting subunit (MYPT) during cell division
Comparison
Mitosis-specific phosphorylation of MYPT vs MYPT from cells in interphase
Design
Preclinical
Authors
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Extends mitotic cytoskeletal regulation; hypothesis-generating for cardiomyocyte division and should not yet change practice.
Mitosis-specific phosphorylation of MYPT increases its binding to myosin II and enhances myosin phosphatase activity, suggesting a regulatory mechanism for stress fiber disassembly during prophase.
Totsukawa et al. (1999) studied Cell division. Mitosis-specific phosphorylation of MYPT vs. MYPT from cells in interphase was evaluated on Binding to myosin II and myosin phosphatase activity. Mitosis-specific phosphorylation of the myosin phosphatase targeting subunit increased its binding to myosin II by two- to threefold and more than doubled myosin phosphatase activity.
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