β‐catenin mediates alteration in cell proliferation, motility and invasion of prostate cancer cells by differential expression of E‐cadherin and protein kinase D1

Syed, Viqar; Mak, Paul; Du, Cheng; Balaji, K.C.

doi:10.1002/jcb.21603

Cited by 42 publications

(62 citation statements)

References 50 publications

(44 reference statements)

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“…We have published previously that down-regulation of PKD1 in fact increases total cellular h-catenin. This provides further corroborative evidence for role of PKD1 in membrane trafficking of h-catenin because membrane h-catenin is decreased in spite of increased total levels of cellular h-catenin when PKD1 expression is reduced (32). However, the exact mechanism of regulation of h-catenin expression by PKD1 remains to be investigated.…”

Section: Effect Of Pkd1 Inhibition On B-catenin Subcellular Localizationsupporting

confidence: 63%

Bryostatin 1 modulates β-catenin subcellular localization and transcription activity through protein kinase D1 activation

Jaggi

Chauhan

et al. 2008

Molecular Cancer Therapeutics

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In recent years, the use of natural products for cancer prevention and treatment has received considerable attention. Bryostatin 1 is a natural macrocyclic lactone and a protein kinase D (PKD) modulator with potent antineoplastic properties that has been used to treat human cancers in clinical trials with limited success. Further understanding the mechanistic basis of Bryostatin 1 action may provide opportunities to improve clinical results of treatment with Bryostatin 1. We identified that PKD1, founding member of PKD family of serine/threonine kinases, modulates E-cadherin/B-catenin activity, which plays an important role in cell integrity, polarity, growth, and morphogenesis. An aberrant expression and localization of E-cadherin/B-catenin has been strongly associated with cancer progression and metastasis. In this study, we examined the effect of Bryostatin 1 treatment on PKD1 activation, B-catenin translocation and transcription activity, and malignant phenotype of prostate cancer cells. Initial activation of PKD1 with Bryostatin 1 leads to colocalization of the cytoplasmic pool of B-catenin with PKD1, trans-Golgi network markers, and proteins involved in vesicular trafficking. Activation of PKD1 by Bryostatin 1 decreases nuclear B-catenin expression and B-catenin/TCF transcription activity. Activation of PKD1 alters cellular aggregation and proliferation in prostate cancer cells associated with subcellular redistribution of E-cadherin and B-catenin. For the first time, we have identified that Bryostatin 1 modulates B-catenin signaling through PKD1, which identifies a novel mechanism to improve efficacy of Bryostatin 1 in clinical settings. [Mol Cancer Ther 2008;7(9):2703 -12]

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Section: Effect Of Pkd1 Inhibition On B-catenin Subcellular Localizationsupporting

confidence: 63%

Bryostatin 1 modulates β-catenin subcellular localization and transcription activity through protein kinase D1 activation

Jaggi

Chauhan

et al. 2008

Molecular Cancer Therapeutics

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“…PRKD1 (protein kinase D1) is also known as protein kinase C mu (atypical PKC), which is a serine/threonine kinase and can be activated by PKC, involving various functions including adhesion, cell motility, and cell proliferation. PKD1 can interact with androgen receptor (AR) and modulated AR function in prostate cancer [42][43][44]. In our project, PRKD1 was down-regulated in PC3 (expression level: 4.5) and DU145 (expression level: 5.4), compared with LNCaP (expression level: 100), showing that mRNA level was decreased in androgen-independent phenotype, which is similar to PRKACB above.…”

Section: Citationsupporting

confidence: 56%

Identification of Mutations, Expression Alterations and Fusion Transcripts by Next Generation RNAseq in Castration-Resistant Prostate Cancer Cell lines with Possible Clinical Relevance

Ma¹,

Miao²,

Peng³

et al. 2017

Next Generat Sequenc & Applic

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Androgen Deprivation Therapy (ADT) would benefit prostate cancer patients initially but cancer cells can eventually develop castration resistance. In this study, we compared androgen-dependent and androgenindependent cell lines to find potential genes associated with acquired resistance to ADT. Using RNAseq, we found 4397 mutations distributed in 2579 genes, out of which, 1574 mutated genes could also be found in prostate cancer tumor samples collected in Cosmic database (http://cancer.sanger.ac.uk/cosmic). We also discovered 157 and 549 genes which were down and up-regulated respectively in both PC3 and DU145 compared to LNCaP. Network analysis resulted in 3 dominant connection notes: GCR/MCR (NR3C1) and PKA-cat kinase (PRKACB) and PKC family (PRKD1). By ChimeraScan analysis, 48, 117 and 60 chimeric transcripts were discovered in DU145, LNCaP and PC3 respectively. Among them, six predicted fusions expressed specifically in androgen-independent cell lines (DU145 and PC3). Some of these gene mutations and transcription alterations have been reported in tumor samples from prostate cancer patients and may have certain associations with acquired resistance to anti-hormone therapy in prostate cancer. A proportion of mutations are enriched in genes involved in immune response pathways, suggesting new targets to develop effective treatments to overcome castration resistance.

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“…1 B and C), suggesting that there might be alterations in proteins involved in cellular adhesion. Since cadherins play an important role in cell-cell adhesion and expression of E-cadherin can suppress tumor cell motility (26,27), we investigated the level of E-cadherin in JMY depleted cells. A marked upregulation of E-cadherin in JMY siRNA treated MCF-7 cells was apparent ( Fig.…”

Section: Resultsmentioning

confidence: 99%

A transcription co-factor integrates cell adhesion and motility with the p53 response

Coutts

Weston

Thangué

2009

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

163

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Despite its obvious importance in tumorigenesis, little information is available on the mechanisms that integrate cell motility and adhesion with nuclear events. JMY is a transcription co-factor that regulates the p53 response. In addition, JMY contains a series of WH2 domains that facilitate in vitro actin nucleation. We show here that the ability of JMY to influence cell motility is dependent, in part, on its control of cadherin expression as well as the WH2 domains. In DNA damage conditions JMY undergoes nuclear accumulation, which drives the p53 transcription response but reduces its influence on cell motility. Consequently, the role of JMY in actin nucleation is less in damaged cells, although the WH2 domains remain functional in the nucleus where they impact on p53 activity. Together, these findings demonstrate a pathway that links the cytoskeleton with the p53 response, and further suggest that the ability of JMY to regulate actin and cadherin is instrumental in coordinating cell motility with the p53 response.actin ͉ cell motility ͉ DNA damage ͉ JMY ͉ WH2

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β‐catenin mediates alteration in cell proliferation, motility and invasion of prostate cancer cells by differential expression of E‐cadherin and protein kinase D1

Cited by 42 publications

References 50 publications

Bryostatin 1 modulates β-catenin subcellular localization and transcription activity through protein kinase D1 activation

Bryostatin 1 modulates β-catenin subcellular localization and transcription activity through protein kinase D1 activation

Identification of Mutations, Expression Alterations and Fusion Transcripts by Next Generation RNAseq in Castration-Resistant Prostate Cancer Cell lines with Possible Clinical Relevance

A transcription co-factor integrates cell adhesion and motility with the p53 response

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