Imaging single CaMKII holoenzymes at work by high-speed atomic force microscopy

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  • Shotaro Tsujioka
    Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Ayumi Sumino
    Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Yutaro Nagasawa
    Department of Physiological Sciences, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193, Japan.
  • Takashi Sumikama
    WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Holger Flechsig
    WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Leonardo Puppulin
    WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Takuya Tomita
    Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa Ishikawa 920-1192, Japan.
  • Yudai Baba
    Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa Ishikawa 920-1192, Japan.
  • Takahiro Kakuta
    WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Tomoki Ogoshi
    WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Kenichi Umeda
    WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Noriyuki Kodera
    WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
  • Hideji Murakoshi
    Department of Physiological Sciences, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193, Japan.
  • Mikihiro Shibata
    Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.

説明

<jats:p> Ca <jats:sup>2+</jats:sup> /calmodulin-dependent protein kinase II (CaMKII) plays a pivotal role in synaptic plasticity. It is a dodecameric serine/threonine kinase that has been highly conserved across metazoans for over a million years. Despite the extensive knowledge of the mechanisms underlying CaMKII activation, its behavior at the molecular level has remained unobserved. In this study, we used high-speed atomic force microscopy to visualize the activity-dependent structural dynamics of rat/hydra/ <jats:italic>C. elegans</jats:italic> CaMKII with nanometer resolution. Our imaging results revealed that the dynamic behavior is dependent on CaM binding and subsequent pT286 phosphorylation. Among the species studies, only rat CaMKIIα with pT286/pT305/pT306 exhibited kinase domain oligomerization. Furthermore, we revealed that the sensitivity of CaMKII to PP2A in the three species differs, with rat, <jats:italic>C. elegans</jats:italic> , and hydra being less dephosphorylated in that order. The evolutionarily acquired features of mammalian CaMKIIα-specific structural arrangement and phosphatase tolerance may differentiate neuronal function between mammals and other species. </jats:p>

収録刊行物

  • Science Advances

    Science Advances 9 (26), eadh1069-, 2023-06-30

    American Association for the Advancement of Science (AAAS)

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