Structural highlights
Function
MICA1_HUMAN Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (Probable). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4.[1] [2]
References
- ↑ Schmidt EF, Shim SO, Strittmatter SM. Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein. J Neurosci. 2008 Feb 27;28(9):2287-97. doi: 10.1523/JNEUROSCI.5646-07.2008. PMID:18305261 doi:http://dx.doi.org/10.1523/JNEUROSCI.5646-07.2008
- ↑ Zucchini D, Caprini G, Pasterkamp RJ, Tedeschi G, Vanoni MA. Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1. Arch Biochem Biophys. 2011 Nov;515(1-2):1-13. doi: 10.1016/j.abb.2011.08.004., Epub 2011 Aug 16. PMID:21864500 doi:http://dx.doi.org/10.1016/j.abb.2011.08.004
