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.
Note on the detailed structural study of CDPK activation, focusing on apicomplexan CAD conformations (CpCDPK, PfCDPK3), offering new insight into a potentially universal activation mechanism for CDPKs.
Note on the discovery that the variable N-terminal domain of CDPK1 controls substrate specificity—offering a new mechanism to engineer signaling specificity in plants.
A 1975 Science paper pioneering the computational prediction of EF-hand calcium-binding motifs in unexpected proteins, revealing evolutionary insights into calcium sensor domains and highlighting structural conservation even in non-calcium-binding proteins.
A 2000 PROTEINS paper exploring the structural modeling of the calmodulin-like domain (CLD) of soybean CDPK-α, revealing unique domain features and potential intramolecular regulatory mechanisms based on homology modeling and experimental validation.
A 1991 Science paper reporting the discovery of a soybean CDPK as a novel class of calcium-dependent kinases, providing structural and evolutionary insights that shaped the understanding of CDPKs as CaM-like autonomous calcium sensors.
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.
A 2006 JMB study presenting the crystal structure of Arabidopsis CDPK’s regulatory domain, revealing a domain-swapped dimer and an unexpected mechanism of calmodulin-like domain (CaM-LD) recognition, challenging classical calmodulin-target models.
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 uncovering the high-resolution structure of the Ca2+-regulatory domain of soybean CDPK-alpha, revealing novel lobe interactions and a pivot-based mechanism, distinct from calmodulin-based models.
Notes on a 1996 Biochemistry paper revealing that activation of CDPK involves intramolecular binding between its calmodulin-like domain (CaM-LD) and junction/autoinhibitor, offering deep insights into Ca2+-regulated protein kinase activation.
Notes on a 2000 Plant Journal paper identifying dual lipid modifications — myristoylation and palmitoylation — as essential for membrane targeting of rice CDPK (OsCDPK2), marking the first report of such dual acylation in plant CDPKs.
Notes on a 2010 JBC paper investigating in vivo phosphorylation of tobacco CDPKs (NtCDPK2 and NtCDPK3) in response to stress, revealing distinct intra- and inter-molecular phosphorylation events, N-terminal-specific regulation, and the critical role of membrane localization.
