Key result
Mouse MIM binds ATP-G-actin with higher affinity (KD = 0.06 μm) than ADP-G-actin (KD = 0.3 μm) via its C-terminal WH2 domain, inhibiting actin filament nucleation in vitro.
Population
Mouse embryos, adult mice, and NIH 3T3 cells
Design
Preclinical
Authors
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MIM may regulate cytoskeletal dynamics in developing cardiac muscle; leaves open its role in human heart disease.
MIM is an ATP-G-actin binding protein that regulates cytoskeletal dynamics in specialized mammalian cell-types, including developing cardiac muscles.
Mattila et al. (2003) studied this question. Mouse MIM protein was evaluated on Actin monomer binding and filament nucleation. Mouse MIM binds ATP-G-actin with higher affinity (KD = 0.06 μm) than ADP-G-actin (KD = 0.3 μm) via its C-terminal WH2 domain, inhibiting actin filament nucleation in vitro.
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