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| | ==Crystal Structure of mouse CARMIL residues 1-668== | | ==Crystal Structure of mouse CARMIL residues 1-668== |
| - | <StructureSection load='4k17' size='340' side='right' caption='[[4k17]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='4k17' size='340' side='right'caption='[[4k17]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4k17]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K17 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k17]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K17 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABU:GAMMA-AMINO-BUTANOIC+ACID'>ABU</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OHB:SALICYLAMIDE'>OHB</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]] 2.895Å</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABU:GAMMA-AMINO-BUTANOIC+ACID'>ABU</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=OHB:SALICYLAMIDE'>OHB</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Carmil, Lrrc16, Lrrc16a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=4k17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k17 OCA], [https://pdbe.org/4k17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k17 RCSB], [https://www.ebi.ac.uk/pdbsum/4k17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k17 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k17 RCSB], [http://www.ebi.ac.uk/pdbsum/4k17 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CARL1_MOUSE CARL1_MOUSE] Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028).<ref>PMID:16054028</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4k17" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Dominguez, R]] | + | [[Category: Dominguez R]] |
| - | [[Category: Zwolak, A]] | + | [[Category: Zwolak A]] |
| - | [[Category: Lipid binding]]
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| - | [[Category: Lipid binding protein]]
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| - | [[Category: Lrr domain]]
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| - | [[Category: Ph domain]]
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| - | [[Category: Phosphatidylinositol]]
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| - | [[Category: Phosphatidylinositol-5-phosphate]]
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| - | [[Category: Phosphatidylserine]]
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| - | [[Category: Plasma membrane]]
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| - | [[Category: Protein-protein interaction]]
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| Structural highlights
Function
CARL1_MOUSE Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028).[1]
Publication Abstract from PubMed
CARMIL is an approximately 1,370-amino-acid cytoskeletal scaffold that has crucial roles in cell motility and tissue development through interactions with cytoskeletal effectors and regulation of capping protein at the leading edge. However, the mechanism of CARMIL leading edge localization is unknown. Here we show that CARMIL interacts directly with the plasma membrane through its amino-terminal region. The crystal structure of CARMIL1-668 reveals that this region harbours a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain. Lipid binding is mediated by the PH domain, but is further enhanced by a central helical domain. Small-angle X-ray scattering reveals that the helical domain mediates antiparallel dimerization, properly positioning the PH domains for simultaneous membrane interaction. In cells, deletion of the PH domain impairs leading edge localization. The results support a direct membrane-binding mechanism for CARMIL localization at the leading edge, where it regulates cytoskeletal effectors and motility.
CARMIL leading edge localization depends on a non-canonical PH domain and dimerization.,Zwolak A, Yang C, Feeser EA, Michael Ostap E, Svitkina T, Dominguez R Nat Commun. 2013 Sep 27;4:2523. doi: 10.1038/ncomms3523. PMID:24071777[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang C, Pring M, Wear MA, Huang M, Cooper JA, Svitkina TM, Zigmond SH. Mammalian CARMIL inhibits actin filament capping by capping protein. Dev Cell. 2005 Aug;9(2):209-21. PMID:16054028 doi:http://dx.doi.org/10.1016/j.devcel.2005.06.008
- ↑ Zwolak A, Yang C, Feeser EA, Michael Ostap E, Svitkina T, Dominguez R. CARMIL leading edge localization depends on a non-canonical PH domain and dimerization. Nat Commun. 2013 Sep 27;4:2523. doi: 10.1038/ncomms3523. PMID:24071777 doi:http://dx.doi.org/10.1038/ncomms3523
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