How Do Kinases Transfer Phosphoryl Groups

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.

Regulation of the ABC Kinases by Phosphorylation: Protein Kinase C as a Paradigm

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.

Regulation of the ABC Kinases by Phosphorylation: Protein Kinase C as a Paradigm

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.

Autonomous Activity of CaMKKβ via Intramolecular Autophosphorylation at Thr482: A Mechanism to Bypass Calcium-Calmodulin Dependency

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.

Autonomous Activity of CaMKKβ via Intramolecular Autophosphorylation at Thr482: A Mechanism to Bypass Calcium-Calmodulin Dependency

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.

The Calmodulin-Fused Kinase (CFK) Family: A Major System Converting Calcium Signals into Protein Phosphorylation in Plants

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.

The Calmodulin-Fused Kinase (CFK) Family: A Major System Converting Calcium Signals into Protein Phosphorylation in Plants

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.

Calmodulin Trapping by CaMKII: A Mechanism for Frequency Decoding of Calcium Signals

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.

Calmodulin Trapping by CaMKII: A Mechanism for Frequency Decoding of Calcium Signals

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.

Dual Role of Calmodulin in CaMKII Autophosphorylation: Decoding Calcium Frequency

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.

Dual Role of Calmodulin in CaMKII Autophosphorylation: Decoding Calcium Frequency

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.

Tobacco Calcium-Dependent Protein Kinases Are Differentially Phosphorylated In Vivo as Part of a Kinase Cascade That Regulates Stress Response

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.

Tobacco Calcium-Dependent Protein Kinases Are Differentially Phosphorylated In Vivo as Part of a Kinase Cascade That Regulates Stress Response

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.

Autophosphorylation-Dependent Activation of a Calcium-Dependent Protein Kinase from Groundnut

Notes on a 1999 ASPS paper analyzing autophosphorylation-dependent activation of a calcium-dependent protein kinase (GnCDPK) from groundnut and its role in substrate phosphorylation.

Autophosphorylation-Dependent Activation of a Calcium-Dependent Protein Kinase from Groundnut

Notes on a 1999 ASPS paper analyzing autophosphorylation-dependent activation of a calcium-dependent protein kinase (GnCDPK) from groundnut and its role in substrate phosphorylation.

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