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 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.
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 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.
