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Heterogeneity in human hippocampal CaMKII transcripts reveals allosteric hub-dependent regulation

https://doi.org/10.1101/721589
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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UCSF Chimera—A visualization system for exploratory research and analysis
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A new potent calmodulin antagonist with arylalkylamine structure: crystallographic, spectroscopic and functional studies
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Oligomeric structure of α-calmodulin-dependent protein kinase II11Edited by A. R. Fersht
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Calcium, Calmodulin, and Calcium-Calmodulin Kinase II: Heartbeat to Heartbeat and Beyond
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A short amino acid sequence able to specify nuclear location
inferredcites →https://doi.org/10.1016/j.bpj.2018.11.006openalex-snapshot
Architectural Dynamics of CaMKII-Actin Networks
inferredcites →https://doi.org/10.1016/j.cell.2005.10.029openalex-snapshot
Structure of the Autoinhibited Kinase Domain of CaMKII and SAXS Analysis of the Holoenzyme
inferredcites →https://doi.org/10.1016/j.cell.2011.07.038openalex-snapshot
A Mechanism for Tunable Autoinhibition in the Structure of a Human Ca2+/Calmodulin- Dependent Kinase II Holoenzyme
inferredcites →https://doi.org/10.1016/j.cell.2014.09.019openalex-snapshot
γCaMKII Shuttles Ca2+/CaM to the Nucleus to Trigger CREB Phosphorylation and Gene Expression
inferredcites →https://doi.org/10.1016/j.gene.2003.08.023openalex-snapshot
Organization and evolution of multifunctional Ca2+/CaM-dependent protein kinase genes
inferredcites →https://doi.org/10.1016/j.jsb.2005.07.007openalex-snapshot
Automated electron microscope tomography using robust prediction of specimen movements
inferredcites →https://doi.org/10.1016/j.jsb.2015.08.008openalex-snapshot
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
inferredcites →https://doi.org/10.1016/s0021-9258(18)41915-1openalex-snapshot
Inhibitory autophosphorylation of multifunctional Ca2+/calmodulin-dependent protein kinase analyzed by site-directed mutagenesis.
inferredcites →https://doi.org/10.1016/s0021-9258(19)38577-1openalex-snapshot
Activation of type II calcium/calmodulin-dependent protein kinase by Ca2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain.
inferredcites →https://doi.org/10.1021/bi00045a027openalex-snapshot
Characterization of pp60c-src Tyrosine Kinase Activities Using a Continuous Assay: Autoactivation of the Enzyme Is an Intermolecular Autophosphorylation Process
inferredcites →https://doi.org/10.1038/ncomms15742openalex-snapshot
The CaMKII holoenzyme structure in activation-competent conformations
inferredcites →https://doi.org/10.1038/nmeth.1353openalex-snapshot
Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)
inferredcites →https://doi.org/10.1038/nmeth.4193openalex-snapshot
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
inferredcites →https://doi.org/10.1038/nrn3192openalex-snapshot
Mechanisms of CaMKII action in long-term potentiation
inferredcites →https://doi.org/10.1038/nsmb.1751openalex-snapshot
Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation
inferredcites →https://doi.org/10.1038/s41598-018-23779-4openalex-snapshot
Analysis of the CaMKIIα and β splice-variant distribution among brain regions reveals isoform-specific differences in holoenzyme formation
inferredcites →https://doi.org/10.1073/pnas.0701656104openalex-snapshot
The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure
inferredcites →https://doi.org/10.1073/pnas.0813013106openalex-snapshot
The δ isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload
inferredcites →https://doi.org/10.1074/jbc.271.47.29619openalex-snapshot
A Peptide Model for Calmodulin Trapping by Calcium/Calmodulin-dependent Protein Kinase II
inferredcites →https://doi.org/10.1074/jbc.273.31.19763openalex-snapshot
Phosphorylation at the Nuclear Localization Signal of Ca2+/Calmodulin-dependent Protein Kinase II Blocks Its Nuclear Targeting
inferredcites →https://doi.org/10.1074/jbc.275.19.14354openalex-snapshot
Three-dimensional Reconstructions of Calcium/Calmodulin-dependent (CaM) Kinase IIα and Truncated CaM Kinase IIα Reveal a Unique Organization for Its Structural Core and Functional Domains
inferredcites →https://doi.org/10.1091/mbc.e06-03-0252openalex-snapshot
CaMKIIβ Association with the Actin Cytoskeleton Is Regulated by Alternative Splicing
inferredcites →https://doi.org/10.1093/emboj/17.19.5598openalex-snapshot
αKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle
inferredcites →https://doi.org/10.1093/emboj/cdf360openalex-snapshot
Alternative splicing modulates the frequency‐dependent response of CaMKII to Ca2+ oscillations
inferredcites →https://doi.org/10.1093/hmg/ddv617openalex-snapshot
Homozygous mutation of PLCZ1 leads to defective human oocyte activation and infertility that is not rescued by the WW-binding protein PAWP
inferredcites →https://doi.org/10.1101/cshperspect.a035147openalex-snapshot
Structural Insights into the Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII)
inferredcites →https://doi.org/10.1107/s0907444909052925openalex-snapshot
PHENIX : a comprehensive Python-based system for macromolecular structure solution
inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot
Features and development of Coot
inferredcites →https://doi.org/10.1111/j.1742-4658.2005.05088.xopenalex-snapshot
Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II
inferredcites →https://doi.org/10.1126/science.1321493openalex-snapshot
Impaired Spatial Learning in α-Calcium-Calmodulin Kinase II Mutant Mice
inferredcites →https://doi.org/10.1126/science.256.5060.1199openalex-snapshot
Calmodulin Trapping by Calcium-Calmodulin-Dependent Protein Kinase
inferredcites →https://doi.org/10.1126/science.279.5348.227openalex-snapshot
Sensitivity of CaM Kinase II to the Frequency of Ca 2+ Oscillations
inferredcites →https://doi.org/10.1126/science.279.5352.870openalex-snapshot
Autophosphorylation at Thr 286 of the α Calcium-Calmodulin Kinase II in LTP and Learning
inferredcites →https://doi.org/10.1128/mcb.16.1.29openalex-snapshot
An alternative, Nonkinase Product of the Brain-Specifically Expressed Ca 2+ /Calmodulin-Dependent Kinase II α Isoform Gene in Skeletal muscle
inferredcites →https://doi.org/10.1172/jci36942openalex-snapshot
Human sperm devoid of PLC, zeta 1 fail to induce Ca2+ release and are unable to initiate the first step of embryo development
inferredcites →https://doi.org/10.1371/journal.pbio.1000426openalex-snapshot
Structure of the CaMKIIδ/Calmodulin Complex Reveals the Molecular Mechanism of CaMKII Kinase Activation
inferredcites →https://doi.org/10.1371/journal.pone.0105191openalex-snapshot
Generation and Behavior Characterization of CaMKIIβ Knockout Mice
inferredcites →https://doi.org/10.1523/jneurosci.15-10-06797.1995openalex-snapshot
Developmental and regional expression of multifunctional Ca2+/calmodulin-dependent protein kinase isoforms in rat brain
inferredcites →https://doi.org/10.3835/plantgenome2014.10.0070openalex-snapshot
HtStuf: High‐Throughput Sequencing to Locate Unknown DNA Junction Fragments
inferredcites →https://doi.org/10.4161/cib.2.1.7426openalex-snapshot
Neuronal CaMKII acts as a structural kinase
inferredcites →https://doi.org/10.7554/elife.01610openalex-snapshot
Activation-triggered subunit exchange between CaMKII holoenzymes facilitates the spread of kinase activity
inferredcites →https://doi.org/10.7554/elife.13405openalex-snapshot
Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II
inferredcites →https://doi.org/10.7554/elife.42166openalex-snapshot
New tools for automated high-resolution cryo-EM structure determination in RELION-3

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/pro.3869openalex-snapshot
Characterization of CaMKIIα holoenzyme stability
inferred← citeshttps://doi.org/10.1073/pnas.2006382117openalex-snapshot
Intrinsically disordered linkers control tethered kinases via effective concentration
inferred← citeshttps://doi.org/10.1111/ejn.14761openalex-snapshot
Functional implications of CaMKII alternative splicing
inferred← citeshttps://doi.org/10.7554/elife.53670openalex-snapshot
Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation
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