An in-depth review of CaMKK signaling, including structural, regulatory, and functional insights into its activation, downstream effects, and implications for disease.
An in-depth review of CaMKK signaling, including structural, regulatory, and functional insights into its activation, downstream effects, and implications for disease.
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 2000 JBC paper dissecting the autoinhibitory mechanism of CaMKK, identifying Ile441 as critical for maintaining the inactive state, and showing that CaM-binding peptide orientation does not dictate relief from autoinhibition — a pivotal insight into CaMKK regulation.
Notes on a 2000 JBC paper dissecting the autoinhibitory mechanism of CaMKK, identifying Ile441 as critical for maintaining the inactive state, and showing that CaM-binding peptide orientation does not dictate relief from autoinhibition — a pivotal insight into CaMKK regulation.
Overview of the plant-specific CDPK-SnRK superfamily, including CDPKs, CRKs, CCaMKs, SnRKs, and their Ca²⁺ regulatory mechanisms. Models of activation and functional diversity of Ca²⁺ decoding mechanisms are discussed.
Overview of the plant-specific CDPK-SnRK superfamily, including CDPKs, CRKs, CCaMKs, SnRKs, and their Ca²⁺ regulatory mechanisms. Models of activation and functional diversity of Ca²⁺ decoding mechanisms are discussed.
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.
A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.
A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.
Notes on a landmark Nature (1999) paper detailing how calmodulin (CaM) adopts a unique binding mode when interacting with CaMKK, revealing an extended 26-residue peptide interface and an opposite binding orientation, distinguishing it from classical CaM-target interactions — a new paradigm in calcium signaling complexes.
