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 1995 Nature paper revealing the structural mechanism of CDK2 activation by cyclinA, focusing on key conformational changes that relieve autoinhibition and organize the catalytic site.
Note on the differential calcium sensitivity among Arabidopsis CDPK isoforms, highlighting the diversity of activation mechanisms and implications for calcium signaling in plants.
Notes on 1998 Cell review discussing kinase phosphoryl transfer mechanisms, conformational dynamics, cofactor roles, and binding motifs. Highlights the debate between associative (SN2) and dissociative (SN1) pathways, with structural evidence for both models.
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 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 landmark review on the ordered, site-specific phosphorylation events governing the maturation, activation, and regulation of ABC kinases — using PKC as a paradigm — with profound insights into kinase life cycles, structural stabilization, and multi-step control mechanisms.
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 landmark structural study revealing how apicomplexan CDPKs (TgCDPK1/3, CpCDPK) undergo dramatic conformational changes upon calcium binding to shift from an autoinhibited to an active state.
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.
A comprehensive study unraveling the molecular dynamics of recoverin’s membrane binding via its calcium-dependent myristoyl switch, highlighting the importance of N-terminal domain conformations and transient C-terminal interactions.
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.
Notes on a 2011 ACS Biochemistry study showing that CaMKKβ, unlike CaMKKα, achieves high autonomous activity via intramolecular autophosphorylation at Thr482, partially releasing itself from autoinhibition and making it Ca2+/CaM-independent — revealing a unique kinase regulation mechanism within the CaMKK family.
Notes on a 2001 Journal of Molecular Biology paper revealing the crystal structure of Ca2+/CaM bound to a CaMKK-derived peptide, highlighting how calmodulin achieves conformational flexibility to accommodate diverse targets — offering a mechanistic basis for how CaM relieves autoinhibition of kinases like CaMKK and mediates calcium signal transduction.
