Structure-Function of the Multifunctional Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII)

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.

Structure-Function of the Multifunctional Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII)

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.

Structure of the Autoinhibited CaMKII Kinase Domain and SAXS Analysis of the Holoenzyme

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.

Structure of the Autoinhibited CaMKII Kinase Domain and SAXS Analysis of the Holoenzyme

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.

A Mechanism for Tunable Autoinhibition in the Structure of Human CaMKII Holoenzyme

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.

A Mechanism for Tunable Autoinhibition in the Structure of Human CaMKII Holoenzyme

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.

The CaMKII Holoenzyme Structure in Activation-Competent Conformation

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.

The CaMKII Holoenzyme Structure in Activation-Competent Conformation

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.

Calmodulin Trapping by CaMKII: A Mechanism for Frequency Decoding of Calcium Signals

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.

Calmodulin Trapping by CaMKII: A Mechanism for Frequency Decoding of Calcium Signals

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.

Dual Role of Calmodulin in CaMKII Autophosphorylation: Decoding Calcium Frequency

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.

Dual Role of Calmodulin in CaMKII Autophosphorylation: Decoding Calcium Frequency

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.

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