8FAF

Unedited Octopus bimaculoides Synaptotagmin 1 C2A at room temperature

Summary for 8FAF

• Entry DOI: 10.2210/pdb8faf/pdb
• Descriptor: Synaptotagmin (2 entities in total)
• Functional Keywords: synaptotagmin 1, c2 domain, rna-editing, exocytosis
• Biological source: Octopus bimaculoides
• Total number of polymer chains: 1
• Total formula weight: 15592.72

Authors

McNeme, S.,Dominguez, M.J.,Birk, M.A.,Rosenthal, J.C.,Sutton, R.B. (deposition date: 2022-11-26, release date: 2023-07-19, Last modification date: 2024-05-22)

Primary citation

Birk, M.A.,Liscovitch-Brauer, N.,Dominguez, M.J.,McNeme, S.,Yue, Y.,Hoff, J.D.,Twersky, I.,Verhey, K.J.,Sutton, R.B.,Eisenberg, E.,Rosenthal, J.J.C.
Temperature-dependent RNA editing in octopus extensively recodes the neural proteome.
Cell, 186:2544-2555.e13, 2023

PubMed Abstract: 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-dependent neurotransmitter release, crystal structures and supporting experiments show that editing alters Ca 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.

PubMed: 37295402
DOI: 10.1016/j.cell.2023.05.004

Experimental method

X-RAY DIFFRACTION (1.85 Å)