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| | ==Crystal structure of mouse CRMP2== | | ==Crystal structure of mouse CRMP2== |
| - | <StructureSection load='5uqc' size='340' side='right' caption='[[5uqc]], [[Resolution|resolution]] 1.78Å' scene=''> | + | <StructureSection load='5uqc' size='340' side='right'caption='[[5uqc]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uqc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UQC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uqc]] is a 2 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=5UQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UQC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</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]] 1.78Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dpysl2, Crmp2, Ulip2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene></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=5uqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqc OCA], [http://pdbe.org/5uqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uqc RCSB], [http://www.ebi.ac.uk/pdbsum/5uqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqc 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=5uqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqc OCA], [https://pdbe.org/5uqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uqc RCSB], [https://www.ebi.ac.uk/pdbsum/5uqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DPYL2_MOUSE DPYL2_MOUSE]] Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.<ref>PMID:22057101</ref> | + | [https://www.uniprot.org/uniprot/DPYL2_MOUSE DPYL2_MOUSE] Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.<ref>PMID:22057101</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: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Francois-Moutal, L]] | + | [[Category: Mus musculus]] |
| - | [[Category: Khanna, M]] | + | [[Category: Francois-Moutal L]] |
| - | [[Category: Khanna, R]] | + | [[Category: Khanna M]] |
| - | [[Category: Perez-Miller, S]] | + | [[Category: Khanna R]] |
| - | [[Category: Signaling protein]]
| + | [[Category: Perez-Miller S]] |
| - | [[Category: Sumoylation]]
| + | |
| - | [[Category: Transcription]]
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| Structural highlights
Function
DPYL2_MOUSE Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.[1]
Publication Abstract from PubMed
The neuronal collapsin response mediator protein 2 (CRMP2) undergoes several posttranslational modifications that codify its functions. Most recently, CRMP2 SUMOylation (addition of small ubiquitin like modifier (SUMO)) was identified as a key regulatory step within a modification program that codes for CRMP2 interaction with, and trafficking of, voltage-gated sodium channel NaV1.7. In this addendum, we illustrate the utility of combining sequence alignment within protein families with structural analysis to identify, from a number of putative SUMOylation sites, those that are most likely to be biologically relevant. Co-opting this principle to CRMP2, we demonstrate that, of three sites predicted to be SUMOylated in CRMP2, only the lysine 374 site is a SUMOylation client. A reduction in NaV1.7 currents was the corollary of the loss of CRMP2 SUMOylation at this site. A 1.78-A-resolution crystal structure of mouse CRMP2 was solved using X-ray crystallography, revealing lysine 374 as buried within the CRMP2 tetramer interface but exposed in the monomer. Since CRMP2 SUMOylation is dependent on phosphorylation, we postulate that this state forces CRMP2 towards a monomer, exposing the SUMO site and consequently, resulting in constitutive regulation of NaV1.7.
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.,Dustrude ET, Perez-Miller S, Francois-Moutal L, Moutal A, Khanna M, Khanna R Channels (Austin). 2017 Feb 28:0. doi: 10.1080/19336950.2017.1299838. PMID:28277940[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wakatsuki S, Saitoh F, Araki T. ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent CRMP2 phosphorylation. Nat Cell Biol. 2011 Nov 6;13(12):1415-23. doi: 10.1038/ncb2373. PMID:22057101 doi:http://dx.doi.org/10.1038/ncb2373
- ↑ Dustrude ET, Perez-Miller S, Francois-Moutal L, Moutal A, Khanna M, Khanna R. A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function. Channels (Austin). 2017 Feb 28:0. doi: 10.1080/19336950.2017.1299838. PMID:28277940 doi:http://dx.doi.org/10.1080/19336950.2017.1299838
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