Notes on a 2002 JBC review dissecting CaMKII’s structure-function relationship, covering autoinhibition, isoform diversity, holoenzyme assembly, autophosphorylation, subunit exchange, and Ca2+/CaM frequency decoding — a foundational reference for understanding this multifunctional kinase as a calcium signal integrator.
Notes on a 2002 JBC review dissecting CaMKII’s structure-function relationship, covering autoinhibition, isoform diversity, holoenzyme assembly, autophosphorylation, subunit exchange, and Ca2+/CaM frequency decoding — a foundational reference for understanding this multifunctional kinase as a calcium signal integrator.
Notes on a 2015 Neuron paper revealing how CaMKII’s dual role as kinase and structural element regulates actin remodeling during synaptic plasticity, showing that autophosphorylation-mediated dissociation from F-actin provides a time window permissive for structural long-term potentiation (sLTP).
Notes on a 2015 Neuron paper revealing how CaMKII’s dual role as kinase and structural element regulates actin remodeling during synaptic plasticity, showing that autophosphorylation-mediated dissociation from F-actin provides a time window permissive for structural long-term potentiation (sLTP).
Notes on a 2005 Cell paper revealing the crystal structure of autoinhibited CaMKII kinase domain and small-angle X-ray scattering (SAXS) analysis of the full holoenzyme, uncovering mechanisms for tight autoinhibition and explaining frequency-dependent activation.
Notes on a 2005 Cell paper revealing the crystal structure of autoinhibited CaMKII kinase domain and small-angle X-ray scattering (SAXS) analysis of the full holoenzyme, uncovering mechanisms for tight autoinhibition and explaining frequency-dependent activation.
Notes on a 2011 Cell paper that reveals the full-length crystal structure of human CaMKII in its autoinhibited state and introduces a tunable mechanism for calcium signal decoding based on linker length-dependent conformational dynamics.
Notes on a 2011 Cell paper that reveals the full-length crystal structure of human CaMKII in its autoinhibited state and introduces a tunable mechanism for calcium signal decoding based on linker length-dependent conformational dynamics.
Notes on a landmark 1998 EMBO paper identifying αKAP as the first anchoring protein for CaM kinase II, revealing how αKAP targets CaMKII to the sarcoplasmic reticulum in skeletal muscle and enables tissue-specific membrane localization and signaling control.
Notes on a landmark 1998 EMBO paper identifying αKAP as the first anchoring protein for CaM kinase II, revealing how αKAP targets CaMKII to the sarcoplasmic reticulum in skeletal muscle and enables tissue-specific membrane localization and signaling control.
Notes on a 2017 Nature Communications paper revealing the 3D structure of the CaMKII holoenzyme in an activation-competent conformation, emphasizing the role of flexible linkers and dimeric kinase domain interactions in regulating activation and frequency decoding.
Notes on a 2017 Nature Communications paper revealing the 3D structure of the CaMKII holoenzyme in an activation-competent conformation, emphasizing the role of flexible linkers and dimeric kinase domain interactions in regulating activation and frequency decoding.
Notes on a 1992 Science paper introducing the concept of ‘calmodulin trapping’ by CaMKII via Thr286 autophosphorylation, establishing a mechanism for potentiating and decoding transient calcium signals through enhanced CaM binding.
Notes on a 1992 Science paper introducing the concept of ‘calmodulin trapping’ by CaMKII via Thr286 autophosphorylation, establishing a mechanism for potentiating and decoding transient calcium signals through enhanced CaM binding.
Note on the seminal 1994 paper unveiling calmodulin’s dual role in CaMKII autophosphorylation and proposing a model for calcium frequency decoding in neurons. Includes reflections on CDPK parallels and a comparative framework for calcium signaling kinases.
