basic FUNCTION
| modulating association of tropomyosin with the spectrin-actin complex in the erythrocyte membrane skeleton |
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actin-capping protein that interacts with tropomyosin (TM) at the pointed end of actin filaments |
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novel regulator of skeletal muscle physiology ( |
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capping protein that specify thin filament lengths by controlling actin dynamics at pointed ends ( |
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TMOD3 and TMOD4 compensate for the absence of TMOD1 structurally but not functionally |
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TMOD1-TMOD3 but not TMOD4 nucleate actin filament assembly |
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also required for proper myofibril formation |
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TMOD1 and TMOD2 have mechanistically distinct inhibitory roles in neurite formation, likely mediated via different effects on F-actin dynamics and via differential localizations during early neuritogenesis |
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is an actin-capping protein that binds to the two tropomyosins (TM) at the pointed end of the actin filament to prevent further actin polymerization and depolymerization |
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TMOD1 is involved in neuronal differentiation for proper neurite formation and outgrowth, and TMOD2 inhibits these processes |
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TMOD1, TMOD3, TMOD4 are novel regulators of actomyosin crossbridge formation and muscle contractility |
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in skeletal muscle TMOD1 is a pointed-end capping and tropomyosin-binding protein that controls thin-filament assembly, stability, and lengths |
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is a protein that binds and caps the pointed ends of actin filaments in erythroid and nonerythoid cell types |
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TMOD1, TMOD2, TMOD3 regulates the length of actin filaments by capping the pointed ends in a tropomyosin (TM)-dependent manner |