1.14.13.225: F-actin monooxygenase
This is an abbreviated version!
For detailed information about F-actin monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.225
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1.14.13.225
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plexins
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calponin
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semaphorin-plexin
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sema3a
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plexa
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semaphorin3a
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rab8
- 1.14.13.225
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plexins
- calponin
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semaphorin-plexin
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sema3a
- plexa
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semaphorin3a
- rab8
Reaction
Synonyms
MICAL, MICAL-1, MICAL-2, MICAL1, Mical2, MICAL2PV, MICAL3
ECTree
1.14.13.225 F-actin monooxygenaseAdvanced search results
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results (General Information
General Information on EC 1.14.13.225 - F-actin monooxygenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
the catalytic efficiency of MICAL3 increases on adding F-actin only when the CH domain is available. But this does not occur when two residues, Glu213 and Arg530, are mutated in the FMO and CH domains, respectively
physiological function
additional information
physiological function
F-actin is a direct and specific substrate for Mical. The reaction alters actin at a specific amino acid residue disrupting actin-actin associations and fragmenting filaments. The modified actin no longer polymerizes normally. Mical modifies the pointed-end of actin proteins, and not the fast-growing, membrane-proximal barbed-end. Therefore actin reassembly and branching follows Semaphorin/Plexin/Mical-mediated F-actin collapse
physiological function
F-actin is efficiently dismantled through a post-translational-mediated synergism between cofilin and the actin-oxidizing enzyme Mical. Mical-mediated oxidation of actin improves cofilin binding to filaments, where their combined effect dramatically accelerates F-actin disassembly compared with either effector alone. This synergism is also necessary and sufficient for F-actin disassembly in vivo, magnifying the effects of both Mical and cofilin on cellular remodelling, axon guidance and Semaphorin-Plexin repulsion
physiological function
Mical is both necessary and sufficient for semaphorin-plexin mediated F-actin reorganization in vivo. Mical directly binds F-actin and disassembles both individual and bundled actin filaments. Mical utilizes its redox activity to alter F-actin dynamics in vivo and in vitro
physiological function
Mical oxidizes actin stereo-specifically to generate actin Met-44-R-sulfoxide. Methionine sulfoxide reductase enzyme SelR opposes Mical redox activity and Semaphorin/Plexin repulsion to direct multiple actin-dependent cellular behaviors in vivo
physiological function
MICAL1 gene disruption in MDA-MB-231 cells knocks out protein expression, which affects F-actin organization, cell size and motility. MICAL1 deletion significantly affects the expression of over 700 genes, with the majority being reduced in their expression levels. Receptor regulator activity is the most significant negatively enriched molecular function gene set. MICAL1 deletion on is also associated with changes in the expression of several serum-response factor regulated genes. MICAL1 disruption attenuates breast cancer tumour growth in vivo
physiological function
MICAL isozymes are involved in actin cytoskeleton reorganization through methionine oxidation. The enzyme functions in F-actin disassembly
physiological function
MICAL2 is essential for skeletal muscle homeostasis and functionality. Lack of MICAL2 results in muscle actin defects. MICAL2 upregulation shows a positive impact on skeletal and cardiac muscle commitments
physiological function
splicing isoform MICAL2PV is a tunneling nanotubes (TNT) regulator that suppresses TNT formation and modulates mitochondrial distribution. MICAL2PV interacts with mitochondrial Rho GTPase Miro2 and regulates subcellular mitochondrial trafficking. Downregulation of MICAL2PV enhances survival of cells treated with chemotherapeutical drugs. The monooxygenase domain of MICAL2PV is required for its activity to inhibit TNT formation by depolymerizing F-actin
additional information
the catalytic efficiency of MICAL3 increases on adding F-actin only when the CH domain is available. MICAL3 is structurally highly similar to isozyme MICAL1, which suggests that they may adopt the same catalytic mechanism, but the difference in the relative position of the CH domain produces a difference in F-actin substrate specificity. Interaction analysis of the binding site between the CH domain and the FMO domain in human MICAL3, modeling, overview. The FMO-CH interaction in hMICAL3 is required to increase the catalytic efficiency by conferring specific binding to F-actin. The FMO domain that exhibits monooxygenase activity is localized at the N-terminus of MICAL and is highly conserved among species. The CH domain that is usually found in actin binding proteins is adjacent to the FMO domain and is also highly conserved. CH domains are classified into three types: types 1, 2, and 3. Whereas type 3 CH domains are mainly found in regulatory proteins associated with muscle contraction and signaling proteins, type 1 and 2 CH domains are usually found in cytoskeletal proteins. MICALs have a typical type 2 CH domain
additional information
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the catalytic efficiency of MICAL3 increases on adding F-actin only when the CH domain is available. MICAL3 is structurally highly similar to isozyme MICAL1, which suggests that they may adopt the same catalytic mechanism, but the difference in the relative position of the CH domain produces a difference in F-actin substrate specificity. Interaction analysis of the binding site between the CH domain and the FMO domain in human MICAL3, modeling, overview. The FMO-CH interaction in hMICAL3 is required to increase the catalytic efficiency by conferring specific binding to F-actin. The FMO domain that exhibits monooxygenase activity is localized at the N-terminus of MICAL and is highly conserved among species. The CH domain that is usually found in actin binding proteins is adjacent to the FMO domain and is also highly conserved. CH domains are classified into three types: types 1, 2, and 3. Whereas type 3 CH domains are mainly found in regulatory proteins associated with muscle contraction and signaling proteins, type 1 and 2 CH domains are usually found in cytoskeletal proteins. MICALs have a typical type 2 CH domain
