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| | <StructureSection load='5le0' size='340' side='right'caption='[[5le0]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='5le0' size='340' side='right'caption='[[5le0]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5le0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LE0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LE0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5le0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LE0 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MICAL1, MICAL, NICAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5le0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5le0 OCA], [http://pdbe.org/5le0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5le0 RCSB], [http://www.ebi.ac.uk/pdbsum/5le0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5le0 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5le0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5le0 OCA], [https://pdbe.org/5le0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5le0 RCSB], [https://www.ebi.ac.uk/pdbsum/5le0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5le0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MICA1_HUMAN 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.<ref>PMID:18305261</ref> <ref>PMID:21864500</ref> | + | [https://www.uniprot.org/uniprot/MICA1_HUMAN 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.<ref>PMID:18305261</ref> <ref>PMID:21864500</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hammich, H]] | + | [[Category: Hammich H]] |
| - | [[Category: Houdusse, A]] | + | [[Category: Houdusse A]] |
| - | [[Category: Pylypenko, O]] | + | [[Category: Pylypenko O]] |
| - | [[Category: Mical]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| 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]
Publication Abstract from PubMed
Cytokinetic abscission, the terminal step of cell division, crucially depends on the local constriction of ESCRT-III helices after cytoskeleton disassembly. While the microtubules of the intercellular bridge are cut by the ESCRT-associated enzyme Spastin, the mechanism that clears F-actin at the abscission site is unknown. Here we show that oxidation-mediated depolymerization of actin by the redox enzyme MICAL1 is key for ESCRT-III recruitment and successful abscission. MICAL1 is recruited to the abscission site by the Rab35 GTPase through a direct interaction with a flat three-helix domain found in MICAL1 C terminus. Mechanistically, in vitro assays on single actin filaments demonstrate that MICAL1 is activated by Rab35. Moreover, in our experimental conditions, MICAL1 does not act as a severing enzyme, as initially thought, but instead induces F-actin depolymerization from both ends. Our work reveals an unexpected role for oxidoreduction in triggering local actin depolymerization to control a fundamental step of cell division.
Oxidation of F-actin controls the terminal steps of cytokinesis.,Fremont S, Hammich H, Bai J, Wioland H, Klinkert K, Rocancourt M, Kikuti C, Stroebel D, Romet-Lemonne G, Pylypenko O, Houdusse A, Echard A Nat Commun. 2017 Feb 23;8:14528. doi: 10.1038/ncomms14528. PMID:28230050[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Fremont S, Hammich H, Bai J, Wioland H, Klinkert K, Rocancourt M, Kikuti C, Stroebel D, Romet-Lemonne G, Pylypenko O, Houdusse A, Echard A. Oxidation of F-actin controls the terminal steps of cytokinesis. Nat Commun. 2017 Feb 23;8:14528. doi: 10.1038/ncomms14528. PMID:28230050 doi:http://dx.doi.org/10.1038/ncomms14528
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