Organization and evolution of multifunctional Ca2+/CaM-dependent protein kinase genes

Tombes, Robert M.; Faison, Milton O.; Turbeville, James M.

doi:10.1016/j.gene.2003.08.023

Cited by 198 publications

(209 citation statements)

References 116 publications

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“…11, 12 Recently, it has been shown that in double-knockout mice that had specific and complete deletion of both CaMKIIγ and δ, cardiac myocytes are protected against cardiac dysfunction but that calcineurin-dependent cardiac hypertrophy develops, which is associated with profound hypophosphorylation of typical CaMKII phosphorylation targets. This doubleknockout model also highlights the importance of CaMKII inhibition and CaMKII phosphorylation-dependent mechanisms under pathological conditions.…”

Section: Discussionmentioning

confidence: 99%

Ca2+/Calmodulin-Dependent Protein Kinase II γ-Dependent Serine727 Phosphorylation Is Required for TMEM16A Ca2+-Activated Cl− Channel Regulation in Cerebrovascular Cells

Lin

Yuan

et al. 2018

Circ J

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Section: Discussionmentioning

confidence: 99%

Ca2+/Calmodulin-Dependent Protein Kinase II γ-Dependent Serine727 Phosphorylation Is Required for TMEM16A Ca2+-Activated Cl− Channel Regulation in Cerebrovascular Cells

Lin

Yuan

et al. 2018

Circ J

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“…CaMKII isoforms can associate to form either homo-or heteromultimeric holoenzyme composed of 10-14 subunits. In mammals, CaMKII isoforms are encoded by four different genes (α, β, γ, δ) which share extensive sequence homology and structure [135]. CaMKII transcripts are in turn subject to extensive alternative splicing, resulting in kinases with variable domains and specific cellular functions.…”

Section: Decrease Of Camkiiγ and Increase Of Camk Iiδmentioning

confidence: 99%

“…Although ubiquitously expressed, CaMKII isoforms have a distinct pattern of expression in different tissue beds. Distribution of three distinct α and seven distinct β splice variants are mainly limited to the central nervous system where they are estimated to comprise up to 1% to 2% of the total protein in the forebrain and hippocampus, respectively [41,135]. In the brain, CaMKII is critical for regulating synaptic and behavioral plasticity and possibly memory [33].…”

Section: Decrease Of Camkiiγ and Increase Of Camk Iiδmentioning

confidence: 99%

The non-excitable smooth muscle: Calcium signaling and phenotypic switching during vascular disease

House

Potier

Bisaillon

et al. 2008

Pflugers Arch - Eur J Physiol

221

207

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Calcium (Ca 2+ ) is a highly versatile second messenger that controls vascular smooth muscle cell (VSMC) contraction, proliferation, and migration. By means of Ca 2+ permeable channels, Ca 2+ pumps and channels conducting other ions such as potassium and chloride, VSMC keep intracellular Ca 2+ levels under tight control. In healthy quiescent contractile VSMC, two important components of the Ca 2+ signaling pathways that regulate VSMC contraction are the plasma membrane voltageoperated Ca 2+ channel of the high voltage-activated type (L-type) and the sarcoplasmic reticulum Ca 2+ release channel, Ryanodine Receptor (RyR). Injury to the vessel wall is accompanied by VSMC phenotype switch from a contractile quiescent to a proliferative motile phenotype (synthetic phenotype) and by alteration of many components of VSMC Ca 2+ signaling pathways. Specifically, this switch that culminates in a VSMC phenotype reminiscent of a non-excitable cell is characterized by loss of L-type channels expression and increased expression of the low voltage-activated (T-type) Ca 2+ channels and the canonical transient receptor potential (TRPC) channels. The expression levels of intracellular Ca 2+ release channels, pumps and Ca 2+ -activated proteins are also altered: the proliferative VSMC lose the RyR3 and the sarcoplasmic/endoplasmic reticulum Ca 2+ ATPase isoform 2a pump and reciprocally regulate isoforms of the ca 2+ /calmodulin-dependent protein kinase II. This review focuses on the changes in expression of Ca 2+ signaling proteins associated with VSMC proliferation both in vitro and in vivo. The physiological implications of the altered expression of these Ca 2+ signaling molecules, their contribution to VSMC dysfunction during vascular disease and their potential as targets for drug therapy will be discussed.

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“…The four isoforms of CaMKII (␣, ␤, ␦, and ␥) are encoded by different genes, which display distinct but overlapping expression patterns (12). The ␣ and ␤ isoforms are almost exclusively expressed in the brain, whereas the ␦ and ␥ isoforms are expressed more ubiquitously.…”

mentioning

confidence: 99%

The δ isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload

Backs

Neef

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

392

360

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Acute and chronic injuries to the heart result in perturbation of intracellular calcium signaling, which leads to pathological cardiac hypertrophy and remodeling. Calcium/calmodulin-dependent protein kinase II (CaMKII) has been implicated in the transduction of calcium signals in the heart, but the specific isoforms of CaMKII that mediate pathological cardiac signaling have not been fully defined. To investigate the potential involvement in heart disease of CaMKII␦, the major CaMKII isoform expressed in the heart, we generated CaMKII␦-null mice. These mice are viable and display no overt abnormalities in cardiac structure or function in the absence of stress. However, pathological cardiac hypertrophy and remodeling are attenuated in response to pressure overload in these animals. Cardiac extracts from CaMKII␦-null mice showed diminished kinase activity toward histone deacetylase 4 (HDAC4), a substrate of stress-responsive protein kinases and suppressor of stress-dependent cardiac remodeling. In contrast, phosphorylation of the closely related HDAC5 was unaffected in hearts of CaMKII␦-null mice, underscoring the specificity of the CaMKII␦ signaling pathway for HDAC4 phosphorylation. We conclude that CaMKII␦ functions as an important transducer of stress stimuli involved in pathological cardiac remodeling in vivo, which is mediated, at least in part, by the phosphorylation of HDAC4. These findings point to CaMKII␦ as a potential therapeutic target for the maintenance of cardiac function in the setting of pressure overload.histone deacetylase 4 (HDAC4) ͉ calcium signaling ͉ excitation contraction coupling (EC coupling) ͉ thoracic aortic constriction (TAC) ͉ CaM Kinase II inhibitory peptide (AC3-I)

show abstract

Organization and evolution of multifunctional Ca2+/CaM-dependent protein kinase genes

Cited by 198 publications

References 116 publications

Ca<sup>2+</sup>/Calmodulin-Dependent Protein Kinase II γ-Dependent Serine727 Phosphorylation Is Required for TMEM16A Ca<sup>2+</sup>-Activated Cl<sup>−</sup> Channel Regulation in Cerebrovascular Cells

Ca<sup>2+</sup>/Calmodulin-Dependent Protein Kinase II γ-Dependent Serine727 Phosphorylation Is Required for TMEM16A Ca<sup>2+</sup>-Activated Cl<sup>−</sup> Channel Regulation in Cerebrovascular Cells

The non-excitable smooth muscle: Calcium signaling and phenotypic switching during vascular disease

The δ isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload

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