Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain

Kuret, Jeff; Johnson, G.; Cha, Donald; Christenson, Erik; Demaggio, Anthony J.; Hoekstra, Merl F.

doi:10.1046/j.1471-4159.1997.69062506.x

Cited by 84 publications

(56 citation statements)

References 32 publications

(42 reference statements)

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“…Isoforms Ckiδ and ε preferentially associate with the former whereas Ckiα predominates in the latter [22]. Consistent with these observations, Ckiα copurifies with paired helical filaments from AD brain, composing ∼0.3% (w/w) of affinity purified preparations [25]. Because CK1 isoforms are expressed widely in tissues, including muscle [26], they may modulate tau phosphorylation and aggregation state in s-IBM as well as AD.…”

supporting

confidence: 62%

“…To further characterize s-IBM lesions with respect to tau protein and CK1 isoforms, tissue sections were stained with primary antibodies PHF1 [16], 128a [15,22,25], Ckiε [22], and C19 [22], and subjected to single-label confocal fluorescence microscopy as described previously [22]. PHF1 is a mouse monoclonal antibody that binds tau phosphorylated at residues Ser396 and Ser404 [40].…”

mentioning

confidence: 99%

“…C19 (Santa Cruz Biotech, CA) is a goat polyclonal IgG recognizing the C-terminus of human Ckiα isoforms. These antibodies, which have been characterized for binding specificity by immunoblot analysis [22,25], have been used for double label staining of AD lesions [22]. All primary antibody labelings were conducted as described previously for 16 h at room temperature [22].…”

mentioning

confidence: 99%

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Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis

Kannanayakal

Mendell

Kuret

2008

Neuroscience Letters

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Inclusion body myositis and Alzheimer's disease are age-related disorders characterized in part by the appearance of intracellular lesions composed of filamentous aggregates of the microtubuleassociated protein tau. Abnormal tau phosphorylation accompanies tau aggregation and may be an upstream pathological event in both diseases. Enzymes implicated in tau hyperphosphorylation in Alzheimer's disease include members of the casein kinase-1 family of phosphotransferases, a group of structurally related protein kinases that frequently function in tandem with the ubiquitin modification system. To determine whether casein kinase-1 isoforms associate with degenerating muscle fibers of inclusion body myositis, muscle biopsy sections isolated from sporadic disease cases were subjected to double-label fluorescence immunohistochemistry using selective anti-casein kinase 1 and anti-phospho-tau antibodies. Results showed that the alpha isoform of casein kinase 1, but not the delta or epsilon isoforms, stained degenerating muscle fibers in all eight inclusion body myositis cases examined. Staining was almost exclusively localized to phospho-tau bearing inclusions. These findings, which extend the molecular similarities between inclusion body myositis muscle and Alzheimer's disease brain, implicate casein kinase-1 alpha as one of the phosphotransferases potentially involved in tau hyperphosphorylation. KeywordsInclusion body myositis; Alzheimer's disease; tau protein; protein phosphorylation; protein kinases; casein kinase 1; immunohistochemistry Sporadic inclusion body myositis (s-IBM) is a progressive muscle disease that leads to atrophy of specific muscle groups [12]. Characteristic histopathological findings include vacuolar degeneration of muscle fibers and mononuclear cell inflammation [3]. s-IBM muscle also shares pathobiochemical features with affected neurons in Alzheimer's disease (AD), including the accumulation of β-amyloid peptide [4,32] and the formation of intracellular filamentous inclusions composed of the microtubule associated protein tau [5]. In both s-IBM and AD, the tau proteins incorporated into filaments contain elevated stoichiometries of phosphorylation [23,24] and ubiquitination [6,20]. Depending on the sites occupied, tau hyperphosphorylation

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confidence: 62%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis

Kannanayakal

Mendell

Kuret

2008

Neuroscience Letters

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“…A variety of other studies have provided strong support for a role of CK1 isoforms, particularly CK1␦ and CK1⑀, in diverse cellular processes such as regulation of Wnt signaling and of the circadian clock (7)(8)(9)(10)(11)(13)(14)(15). CK1␦ and CK1⑀ have also been implicated in the pathophysiology of Alzheimer's disease (28,33,34). Regulation of CK1⑀ (and possibly CK1␦) by autophosphorylation and transient dephosphorylation by calcineurin may play an important role in the regulation of these other processes that involve the enzyme.…”

Section: Figmentioning

confidence: 99%

Mechanism of Regulation of Casein Kinase I Activity by Group I Metabotropic Glutamate Receptors

Liu¹,

Virshup²,

Nairn³

et al. 2002

Journal of Biological Chemistry

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Previously, we reported that (S)-3,5-dihydroxypenylglycine (DHPG), an agonist for group I metabotropic glutamate receptors (mGluRs), stimulates CK1 and Cdk5 kinase activities in neostriatal neurons, leading to enhanced phosphorylation, respectively, of Ser-137 and Thr-75 of DARPP-32 (dopamine and cAMP-regulated phosphoprotein, 32 kDa). We have now investigated the signaling pathway that leads from mGluRs to casein kinase 1 (CK1) activation. In mouse neostriatal slices, the effect of DHPG on phosphorylation of Ser-137 or Thr-75 of DARPP-32 was blocked by the phospholipase C␤ inhibitor U73122, the Ca 2؉ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N,N-tetraacetic acid (BAPTA/ AM), and the calcineurin inhibitor cyclosporin A. In neuroblastoma N2a cells, the effect of DHPG on the activity of transfected HA-tagged CK1⑀ was blocked by BAPTA/AM and cyclosporin A. In neostriatal slices, the effect of DHPG on Cdk5 activity was also abolished by BAPTA/AM and cyclosporin A, presumably through blocking activation of CK1. Metabolic labeling studies and phosphopeptide mapping revealed that a set of C-terminal sites in HA-CK1⑀ were transiently dephosphorylated in N2a cells upon treatment with DHPG, and this was blocked by cyclosporin A. A mutant CK1⑀ with a nonphosphorylatable C-terminal domain was not activated by DHPG. Together, these studies suggest that DHPG activates CK1⑀ via Ca 2؉ -dependent stimulation of calcineurin and subsequent dephosphorylation of inhibitory C-terminal autophosphorylation sites. Casein kinase 1 (CK1)1 was one of the first serine/threonine protein kinases to be isolated and characterized. There are at least seven mammalian CK1 isoforms (␣, ␤, ␥1, ␥2, ␥3, ␦, and ⑀ (1, 2)), and distinct CK1 family members are likely to have a variety of roles in eukaryotic cells. An increasing number of potential physiologic substrates for CK1 isoforms have been identified. CK1␣ phosphorylates M1 and M3 muscarinic receptors and rhodopsin in an agonist-dependent manner (3, 4). CK1⑀ and CK1␦ phosphorylate N-terminal residues of p53 in vitro and in vivo, and DNA-damaging drugs enhance this activity (4 -6). CKI⑀ is an important regulator of ␤-catenin in the Wnt pathway; CKI⑀ mimicked Wnt in inducing a secondary axis in Xenopus, stabilizing ␤-catenin, and stimulating ␤-catenin-dependent gene transcription (7-11). In Drosophila, the double-time gene product, a CK1⑀ homolog, has been found to interact with dPER and regulate circadian cycle length (12). CK1␦ and CK1⑀ have also both been implicated in the regulation of the circadian clock in mammals (13-15).CK1 family members contain a highly related, central kinase domain that is flanked by N-and C-terminal extensions of variable length. The amino acid sequences of the C-terminal extensions are in general not highly related. However, the 124-amino acid C-terminal domain of mammalian CK1⑀ is 50% identical to that of CK1␦. Notably, several in vitro studies have shown that the activities of CK1␦ and CK1⑀ are regulated by autophosphorylation of their respective C-terminal domains (...

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“…For example, tyrosine phosphorylation of tau can induce significant conformational changes (Fabian et al, 1994). In the model, this suggests that sites previously inaccessible to proline-directed kinases such as cdc-2 like kinases (cdk5), and MAP kinases, together with CK1, a non-proline-directed kinase (Kuret et al, 1997), may become available for aberrant hyperphosphorylation. It should be noted that abnormally activated cdk5 kinase, a principal mammalian neuronal kinase regulating a range of neuronal functions from migration during neurogenesis to mature synaptic function and neuronal survival, has been implicated in tau hyperphosphorylation and tangle formation in AD (Patrick et al, 1999).…”

Section: Does the Model Offer Clues As To The Factors Responsible Formentioning

confidence: 99%

Squid (Loligo pealei) Giant Fiber System: A Model for Studying Neurodegeneration and Dementia?

Grant

Zheng

Pant

2006

The Biological Bulletin

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Abstract. In many neurodegenerative disorders that lead to memory loss and dementia, the brain pathology responsible for neuronal loss is marked by accumulations of proteins in the form of extracellular plaques and intracellular filamentous tangles, containing hyperphosphorylated cytoskeletal proteins. These are assumed to arise as a consequence of deregulation of a normal pattern of topographic phosphorylation-that is, an abnormal shift of cytoskeletal protein phosphorylation from the normal axonal compartment to cell bodies. Although decades of studies have been directed to this problem, biochemical approaches in mammalian systems are limited: neurons are too small to permit separation of cell body and axon compartments. Since the pioneering studies of Hodgkin and Huxley on the giant fiber system of the squid, however, the stellate ganglion and its giant axons have been the focus of a large literature on the physiology and biochemistry of neuron function. This review concentrates on a host of studies in our laboratory and others on the factors regulating compartment-specific patterns of cytoskeletal protein phosphorylation (primarily neurofilaments) in an effort to establish a normal baseline of information for further studies on neurodegeneration. On the basis of these data, a model of topographic regulation is proposed that offers several possibilities for further studies on potential sites of deregulation that may lead to pathologies resembling those seen in mammalian and human brains showing neurodegeneration, dementia, and neuronal cell death.

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Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain

Cited by 84 publications

References 32 publications

Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis

Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis

Mechanism of Regulation of Casein Kinase I Activity by Group I Metabotropic Glutamate Receptors

Squid (Loligo pealei) Giant Fiber System: A Model for Studying Neurodegeneration and Dementia?

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