8faf
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Unedited Octopus bimaculoides Synaptotagmin 1 C2A at room temperature== | |
+ | <StructureSection load='8faf' size='340' side='right'caption='[[8faf]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[8faf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Octopus_bimaculoides Octopus bimaculoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FAF FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=8faf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8faf OCA], [https://pdbe.org/8faf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8faf RCSB], [https://www.ebi.ac.uk/pdbsum/8faf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8faf ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A0A0L8IHK9_OCTBM A0A0L8IHK9_OCTBM] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | In poikilotherms, temperature changes challenge the integration of physiological function. Within the complex nervous systems of the behaviorally sophisticated coleoid cephalopods, these problems are substantial. RNA editing by adenosine deamination is a well-positioned mechanism for environmental acclimation. We report that the neural proteome of Octopus bimaculoides undergoes massive reconfigurations via RNA editing following a temperature challenge. Over 13,000 codons are affected, and many alter proteins that are vital for neural processes. For two highly temperature-sensitive examples, recoding tunes protein function. For synaptotagmin, a key component of Ca(2+)-dependent neurotransmitter release, crystal structures and supporting experiments show that editing alters Ca(2+) binding. For kinesin-1, a motor protein driving axonal transport, editing regulates transport velocity down microtubules. Seasonal sampling of wild-caught specimens indicates that temperature-dependent editing occurs in the field as well. These data show that A-to-I editing tunes neurophysiological function in response to temperature in octopus and most likely other coleoids. | ||
- | + | Temperature-dependent RNA editing in octopus extensively recodes the neural proteome.,Birk MA, Liscovitch-Brauer N, Dominguez MJ, McNeme S, Yue Y, Hoff JD, Twersky I, Verhey KJ, Sutton RB, Eisenberg E, Rosenthal JJC Cell. 2023 Jun 8;186(12):2544-2555.e13. doi: 10.1016/j.cell.2023.05.004. Epub , 2023 Jun 8. PMID:37295402<ref>PMID:37295402</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 8faf" style="background-color:#fffaf0;"></div> |
- | [[Category: Birk | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
+ | [[Category: Large Structures]] | ||
+ | [[Category: Octopus bimaculoides]] | ||
+ | [[Category: Birk MA]] | ||
+ | [[Category: Dominguez MJ]] | ||
+ | [[Category: McNeme S]] | ||
+ | [[Category: Rosenthal JC]] | ||
+ | [[Category: Sutton RB]] |
Revision as of 06:13, 19 July 2023
Unedited Octopus bimaculoides Synaptotagmin 1 C2A at room temperature
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