Structural features of Ca2+/calmodulin-dependent protein kinase II revealed by electron microscopy.

Kanaseki, Takeshi; Ikeuchi, Yôko; Sugiura, Hiroko; Yamauchi, Takashi

doi:10.1083/jcb.115.4.1049

Cited by 219 publications

(143 citation statements)

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“…It is normally associated in a complex with the calcium carrier calmodulin and is coded then as CaMKII. Kanaseki et al (1991) published excellent observations of kinase II by electron microscopy. The molecule is bulky, so that the images come out well defined (Fig.1).…”

Section: On Kinase IImentioning

confidence: 99%

Spike trains and kinase II for a digital model of long term memory (An exercise in evolutionary constraints)

Marchetti

2000

Hum. Evol.

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Section: On Kinase IImentioning

confidence: 99%

Spike trains and kinase II for a digital model of long term memory (An exercise in evolutionary constraints)

Marchetti

2000

Hum. Evol.

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“…CAMKII is a multisubunit holoenzyme (32). The structure of the holoenzyme has alternatively been referred to as a hub and spoke pattern (33) or a gear and foot pattern (34) and enables a unique autoregulatory mechanism (33). In resting cells, the average Ca 2ϩ concentration is less than 100 nM, and the calmodulin concentration is ϳ10 M. The autoinhibitory domain (AID) of CAMKII interacts with its own catalytic domain resulting in the autoinhibition of catalytic activity.…”

Section: Fig 5 Disease Information In Uniprotkb/swiss-prot Entries:mentioning

confidence: 99%

The Annotation of Both Human and Mouse Kinomes in UniProtKB/Swiss-Prot

Quintaje

Orchard

2008

Molecular & Cellular Proteomics

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In the late 1950s, the role of reversible phosphorylation in enzymatic regulation was recognized by Fischer et al. (1). Phosphorylation events are most commonly mediated by protein kinases, which transfer the ␥-phosphate from nucleotides, usually ATP, via a phosphoester bond (O-phosphate) to the hydroxyl side chain of serine, threonine, or tyrosine residues on their protein substrates. Phosphates are bulky, negatively charged groups, and their addition to a protein can result in a profound change in its interactions with other molecules or subcellular location and/or to a conformational change of the protein itself. Kinase-mediated protein phosphorylation can be reversed through dephosphorylation after which the protein switches back to its original charge state and conformation. As protein conformation often determines function, the phosphorylation event may be considered a type of molecular switch, turning the activity of the molecule on or off. These reversible and dynamic phosphorylation events are under tight control, being governed by the opposing activities of protein kinases and protein phosphatases.Eukaryotic protein kinases (ePKs) 1 play a key role in cell communication pathways and in the transmission of information from outside the cell or between subcellular components within the cell. The ePKs constitute one of the largest mammalian gene families comprising ϳ1.7-2.5% of genes in eukaryotic genomes. Most protein kinases belong to a single superfamily, containing a conserved ePK catalytic domain that consists of a mainly ␤-sheet, NH 2 -terminal subdomain and a larger ␣-helical COOH-terminal subdomain with the ATP-binding pocket situated between the two subdomains. Serine/threonine protein kinases constitute the majority of kinases (67%) within the human kinome; however, tyrosine protein kinases (17%) also play a key role in signaling mechanisms, particularly in cell-cell communication in multicellular organisms (2). The remainder, the atypical protein kinases (aPKs), lack sequence similarity to the ePK catalytic domain but are known to have catalytic functional activity.From the ‡Swiss-Prot group,

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“…Previous reports suggested a role of CaMkinase II in gastric acid secretion [16,17]. A highly specific inhibitor of CaMki-many peripheral tissues, in contrast to the A and the β isoforms, but seem to be expressed at lower levels than the A and β isonase II, the synthetic KN-62 [18,19], blocked over 3Ϫ60 µM carbachol-stimulated [ 14 C]aminopyrine uptake in isolated rabbit forms [15,26,27]. In contrast to other CaMkinases, the group of CaMkinase II forms holoenzymes from 250 kDa up to over gastric parietal cells and failed to inhibit the histamine-stimulated and forskolin-stimulated pathways [16].…”

mentioning

confidence: 99%

“…A major target for Ca 2ϩ binding is the ubiquitous calmodulin [12Ϫ14]. respectively, which are likely homomeric [26]. The CaMkinase II isoforms γ and δ have only been characterized at the cDNA We recently found γ and δ subunits of Ca 2ϩ /calmodulin-dependent protein kinase II (CaMkinase II) in rat gastric mucosal cells level and have apparent molecular masses of 59 kDa and 60 kDa, respectively [24,25].…”

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Purification and characterization of a Ca²⁺/calmodulin‐dependent protein kinase II from hog gastric mucosa using a protein‐protein affinity chromatographic technique

Fährmann

Möhlig

Schatz

et al. 1998

European Journal of Biochemistry

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A peripheral member of the Ca 2ϩ /calmodulin-dependent protein kinase II (CaMkinase II) group has been purified from hog gastric mucosa with the use of a novel affinity-chromatographic step. For the well known neural isotypes of CaMkinase II, it is proposed that the subunits form holoenzymes through a specific domain at the C-terminus called the 'association domain'. We immobilized a bacterially expressed association domain from CaMkinase II-δ-2 and used it as an affinity column. This matrix was used as the last step in a sequential enzyme purification procedure from hog gastric mucosa and yielded a homogeneous CaMkinase II which showed the typical physical and enzymatic properties of CaMkinase II. The enzyme activity showed a dependence on Ca 2ϩ and calmodulin (apparent K 0.5 ϭ 2.7 µM and K 0.5 ϭ 0.02 µM, respectively). We found a subunit molecular mass of 61 kDa. An apparent native molecular mass of 310 kDa was calculated. The Stokes radius and the sedimentation coefficient were 6.7 nm and 11.2 S, respectively. Moreover, the isolated CaMkinase II was very well inhibited by the CaMkinase-IIspecific inhibitors KN-62 (K i ϭ 0.52 nM) and KT5926 (K i ϭ 0.79 nM). The phosphorylation of several substrates revealed its multifunctionality. The purified CaMkinase II had an apparent K m for Mg-ATP of 24.0 µM and for autocamtide-II of 0.62 µM. CaMkinase II is considered as a strong candidate for regulating vesicle released quanta such as acid, neurotransmitters or insulin.Keywords : calmodulin; Ca 2ϩ /calmodulin-dependent protein kinase II ; protein kinase ; purification; affinity chromatography.In gastric parietal cells, at least three major cellular pathways bachol, histamine and forskolin on acid secretion in isolated rabbit gastric parietal cells with K i values of 0.15, 0.3 and 1 µM, mediate an agonist-induced acid secretion [1, 2]. Stimulation of the histaminic receptor H 2 causes the activation of the cAMP respectively. The main effect seemed to be unspecific on the pH gradient formation level [17]. pathway, followed by an unknown acid-secretion mechanism [3]. Another way of acid secretion is muscarinic M 3 receptorThe Ca 2ϩ /calmodulin-dependent protein kinases II are coded for by four genes. The isoforms are named A, β, γ and δ, all mediated [4Ϫ10], which activates phospholipase C, resulting in cleavage of phosphatidylinositol 4,5-bisphosphate into inositol established first in neural tissues [20Ϫ25]. The best characterized isoforms are mammalian CaMkinase II-A (50Ϫ54 kDa) 1,4,5-trisphosphate and diacylglycerol. Gastrin also elevates the intracellular calcium concentration [11]. A subsequent rise in and -β (58Ϫ60 kDa), which are rarely found in non-neural tissues. Both isotypes form holoenzymes of 10 and 8 subunits, cytosolic Ca 2ϩ activates Ca 2ϩ -dependent processes. A major target for Ca 2ϩ binding is the ubiquitous calmodulin [12Ϫ14]. respectively, which are likely homomeric [26]. The CaMkinase II isoforms γ and δ have only been characterized at the cDNA We recently found γ and δ subunits of Ca 2ϩ /calmodulin...

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Structural features of Ca2+/calmodulin-dependent protein kinase II revealed by electron microscopy.

Cited by 219 publications

References 43 publications

Spike trains and kinase II for a digital model of long term memory (An exercise in evolutionary constraints)

Spike trains and kinase II for a digital model of long term memory (An exercise in evolutionary constraints)

The Annotation of Both Human and Mouse Kinomes in UniProtKB/Swiss-Prot

Purification and characterization of a Ca²⁺/calmodulin‐dependent protein kinase II from hog gastric mucosa using a protein‐protein affinity chromatographic technique

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Structural features of Ca2+/calmodulin-dependent protein kinase II revealed by electron microscopy.

Cited by 219 publications

References 43 publications

Spike trains and kinase II for a digital model of long term memory (An exercise in evolutionary constraints)

Spike trains and kinase II for a digital model of long term memory (An exercise in evolutionary constraints)

The Annotation of Both Human and Mouse Kinomes in UniProtKB/Swiss-Prot

Purification and characterization of a Ca2+/calmodulin‐dependent protein kinase II from hog gastric mucosa using a protein‐protein affinity chromatographic technique

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Purification and characterization of a Ca²⁺/calmodulin‐dependent protein kinase II from hog gastric mucosa using a protein‐protein affinity chromatographic technique