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 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.
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.
Notes on a 2017 Scientific Reports study proposing the Calmodulin-Fused Kinase (CFK) family as the principal system for converting calcium signals to protein phosphorylation responses in plants, based on deep phylogenetic analysis tracing their evolutionary origins and functional diversification.
Notes on a 2017 Scientific Reports study proposing the Calmodulin-Fused Kinase (CFK) family as the principal system for converting calcium signals to protein phosphorylation responses in plants, based on deep phylogenetic analysis tracing their evolutionary origins and functional diversification.
Notes on a 2023 The Plant Cell study that introduces a genetically encoded FRET-based biosensor to monitor real-time conformational changes of CDPKs (CPKs) in response to calcium signals in vivo, highlighting distinct calcium sensitivities of CPK21 and CPK23 in stress responses.
Notes on a 2023 The Plant Cell study that introduces a genetically encoded FRET-based biosensor to monitor real-time conformational changes of CDPKs (CPKs) in response to calcium signals in vivo, highlighting distinct calcium sensitivities of CPK21 and CPK23 in stress responses.
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.
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.
Notes on a 2004 JBC paper exploring differential roles of N- and C-lobes in the CaM-like domain (CaM-LD) of CDPK, uncovering distinct Ca2+ affinities and their role in regulating kinase activation through interactions with the junction domain.
Notes on a 2004 JBC paper exploring differential roles of N- and C-lobes in the CaM-like domain (CaM-LD) of CDPK, uncovering distinct Ca2+ affinities and their role in regulating kinase activation through interactions with the junction domain.
