Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a–dependent neurite outgrowth

Greer, Yoshimi Endo; Rubin, Jeffrey S.

doi:10.1083/jcb.201011111

Cited by 49 publications

(81 citation statements)

References 58 publications

(77 reference statements)

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“…3B and data not shown). Previously, we reported that CK1␦ staining was strongest at the centrosome, where it was required for neurite outgrowth induced by Wnt3a (31). Although CK1␦ siRNA did not block PKC phosphorylation following Wnt3a treatment, it did inhibit the pericentrosomal distribution of pPKC (data not shown).…”

Section: Pkc Is Expressed In Esft Cells and Phosphorylated Inmentioning

confidence: 98%

“…Anti-phospho-PKC/ was used at a 1:250 dilution. Double staining of phospho-PKC and pericentrin was performed either with formaldehyde or methanol (MeOH) fixation (31). Total PKC was detected with mouse anti-PKC (1:500 dilution) when cells were fixed in formaldehyde and with rabbit anti-PKC (sc-216, 1:500), which recognizes PKC, when cells were fixed in methanol because of high background with mouse anti-PKC antibody following methanol fixation.…”

Section: Methodsmentioning

confidence: 99%

“…To visualize phalloidin and phospho-PKC/, formaldehyde fixation and staining were performed as previously described (31). Anti-phospho-PKC/ was used at a 1:250 dilution.…”

Section: Methodsmentioning

confidence: 99%

“…A small fraction (10 -15%) of TC-32 cells have long neurites in the basal state, whereas Wnt3a treatment elicits neurite outgrowth in 50 -75% of cells within 3 h. This response is mediated by noncanonical Wnt rather than ␤-catenin signaling and involves a mechanism that requires Fzd3 and Dvl2/3 expression, as well as JNK activation (26). The centrosomal localization of casein kinase 1␦ (CK1␦), a kinase that phosphorylates Dvl proteins, was also shown to be necessary for neurite outgrowth (31), although the functional relevance of Dvl phosphorylation was not established.…”

mentioning

confidence: 99%

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Atypical Protein Kinase Cι Is Required for Wnt3a-dependent Neurite Outgrowth and Binds to Phosphorylated Dishevelled 2

Greer

Fields

Brown

et al. 2013

Journal of Biological Chemistry

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Background: Wnt3a-dependent neurite outgrowth is associated with Dishevelled phosphorylation. Results: PKC is required for Wnt3a-induced neurite extension. PKC binds wild-type Dishevelled, but not an inactive phosphorylation-deficient Dishevelled mutant. Conclusion: PKC mediates Wnt3a-dependent neurite outgrowth; Dishevelled phosphorylation is required for PKC interaction. Significance: PKC has key role in Wnt3a-induced neurite outgrowth; Dvl phosphorylation at defined sites is critical for PKC association.

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Section: Pkc Is Expressed In Esft Cells and Phosphorylated Inmentioning

confidence: 98%

Section: Methodsmentioning

confidence: 99%

“…To visualize phalloidin and phospho-PKC/, formaldehyde fixation and staining were performed as previously described (31). Anti-phospho-PKC/ was used at a 1:250 dilution.…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Atypical Protein Kinase Cι Is Required for Wnt3a-dependent Neurite Outgrowth and Binds to Phosphorylated Dishevelled 2

Greer

Fields

Brown

et al. 2013

Journal of Biological Chemistry

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“…Furthermore, Wnt binding to Frizzled-LRP5/6 induces the phosphorylation of CK1 dependent phosphorylation of p120 (at Ser268 and Ser269) leading to the dissociation of p120 from the E-cadherin complex [230]. This process was shown to be sensitive to the specific CK1 / inhibitor IC261 ( Table 1) [307,308]. IC261 was shown to bind tubulin and act as an inhibitor of microtubules polymerization [308].…”

Section: Connections Between the Wnt-frizzled-lrp5/6 Signalosome And mentioning

confidence: 99%

Wnt/beta-Catenin Signaling and Small Molecule Inhibitors

Voronkov¹,

Krauß²

2012

CPD

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Wnt/ -catenin signaling is a branch of a functional network that dates back to the first metazoans and it is involved in a broad range of biological systems including stem cells, embryonic development and adult organs. Deregulation of components involved in Wnt/ -catenin signaling has been implicated in a wide spectrum of diseases including a number of cancers and degenerative diseases. The key mediator of Wnt signaling, -catenin, serves several cellular functions. It functions in a dynamic mode at multiple cellular locations, including the plasma membrane, where -catenin contributes to the stabilization of intercellular adhesive complexes, the cytoplasm where -catenin levels are regulated and the nucleus where -catenin is involved in transcriptional regulation and chromatin interactions. Central effectors of -catenin levels are a family of cysteine-rich secreted glycoproteins, known as Wnt morphogens. Through the LRP5/6-Frizzled receptor complex, Wnts regulate the location and activity of the destruction complex and consequently intracellularcatenin levels. However, -catenin levels and their effects on transcriptional programs are also influenced by multiple other factors including hypoxia, inflammation, hepatocyte growth factor-mediated signaling, and the cell adhesion molecule E-cadherin. The broad implications of Wnt/ -catenin signaling in development, in the adult body and in disease render the pathway a prime target for pharmacological research and development. The intricate regulation of -catenin at its various locations provides alternative points for therapeutic interventions.

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Neurospora casein kinase 1a recruits the circadian clock protein FRQvia the C‐terminal lobe of its kinase domain

et al. 2022

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Timing by the circadian clock of Neurospora is associated with hyperphosphorylation of frequency (FRQ), which depends on anchoring casein kinase 1a (CK1a) to FRQ. It is not known how CK1a is anchored so that approximately 100 sites in FRQ can be targeted. Here, we identified two regions in CK1a, p1 and p2, that are required for anchoring to FRQ. Mutation of p1 or p2 impairs progressive hyperphosphorylation of FRQ. A p1‐mutated strain is viable but its circadian clock is non‐functional, whereas a p2‐mutated strain is non‐viable. Our data suggest that p1 and potentially also p2 in CK1a provide an interface for interaction with FRQ. Anchoring via p1‐p2 leaves the active site of CK1a accessible for phosphorylation of FRQ at multiple sites.

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Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a–dependent neurite outgrowth

Abstract: Centrosomal localization of kinase-active CK1δ is required for neurite outgrowth in response to Wnt-3a.

Cited by 49 publications

References 58 publications

Atypical Protein Kinase Cι Is Required for Wnt3a-dependent Neurite Outgrowth and Binds to Phosphorylated Dishevelled 2

Atypical Protein Kinase Cι Is Required for Wnt3a-dependent Neurite Outgrowth and Binds to Phosphorylated Dishevelled 2

Wnt/beta-Catenin Signaling and Small Molecule Inhibitors

Neurospora casein kinase 1a recruits the circadian clock protein FRQvia the C‐terminal lobe of its kinase domain

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