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  1. CaMKII autophosphorylation can occur between holoenzymes without subunit exchange

    This article has 10 authors:
    1. Iva Lučić
    2. Léonie Héluin
    3. Pin-Lian Jiang
    4. Alejandro G Castro Scalise
    5. Cong Wang
    6. Andreas Franz
    7. Florian Heyd
    8. Markus C Wahl
    9. Fan Liu
    10. Andrew JR Plested
    This article has been curated by 1 group:
    • Curated by eLife

      eLife assessment

      This manuscript reports the fundamental finding that an oligomeric protein kinase, CaMKII, can be phosphorylated by another molecule of the holoenzyme in a manner that does not involve subunit exchange. The evidence for the main conclusion is compelling, supported by several independent experiments. If independently confirmed in future, the study will stand as having provided a novel regulatory mechanism for the autophosphorylation of this kinase. The work will be of broad interest to molecular and cellular neuroscientists as well as biochemists.

    Reviewed by eLife

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