Protein Kinase D1 Mediates Anchorage-dependent and -independent Growth of Tumor Cells via the Zinc Finger Transcription Factor Snail1

Eiseler, Tim; Köhler, Conny; Nimmagadda, Subbaiah Chary; Jamali, Arsia; Funk, Nancy; Joodi, Golsa; Störz, Peter; Seufferlein, Thomas

doi:10.1074/jbc.m112.370999

Cited by 35 publications

(45 citation statements)

References 37 publications

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“…Stable Caco-2 cells with knockdown of cortactin and PKD1 or nonspecific shRNA scramble cell lines were generated by lentiviral transduction followed by selection with puromycin (6 µg/ml) for 3 weeks. Lentiviruses were generated as described previously (Eiseler et al, 2012). To generate stable Caco-2 cells expressing GFP, cortactin-GFP and cortactin-S298A-GFP with shRNA scramble or vinculin shRNAs, stable cells were transduced with respective lentiviruses and subjected to selection with G418 and puromycin (6 mg/ml, 6 µg/ml) for 3 weeks.…”

Section: Methodsmentioning

confidence: 99%

“…This method allows the determination of protein-protein interactions indicated by an apparent molecular proximity below 10 nm (Eiseler et al, 2012(Eiseler et al, , 2016Gu et al, 2004;Kunkel and Newton, 2009;Oser et al, 2010;Valente et al, 2012;Wille et al, 2014;Wouters et al, 1998;Zeug et al, 2012). The FRET acceptor in a region of interest (ROI) was bleached by an intensive laser line and increase in donor fluorescence, indicating FRET, was measured.…”

Section: Intestinal Permeability Assaymentioning

confidence: 99%

“…Immunofluorescence confocal microscopy and acceptorphotobleach FRET Immunofluorescence and AB-FRET staining was performed as described previously (Eiseler et al, 2012). Experiments were analyzed by confocal laser scanning microscopes LSM710 (Zeiss, Jena, Germany) and TCS SP8-HCS (Leica, Mannheim, Germany) equipped with 40×, 63× Plan Apo oil or water immersion objectives.…”

Section: Intestinal Permeability Assaymentioning

confidence: 99%

“…AB-FRET experiments were performed with transiently transfected or stable Caco-2 cells, fixed, processed and stained as stated previously (Eiseler et al, 2012;Wille et al, 2014). This method allows the determination of protein-protein interactions indicated by an apparent molecular proximity below 10 nm (Eiseler et al, 2012(Eiseler et al, , 2016Gu et al, 2004;Kunkel and Newton, 2009;Oser et al, 2010;Valente et al, 2012;Wille et al, 2014;Wouters et al, 1998;Zeug et al, 2012).…”

Section: Intestinal Permeability Assaymentioning

confidence: 99%

“…Total cell lysates and co-immunoprecipitation experiments (CoIPs) were performed as described previously (Eiseler et al, 2010(Eiseler et al, , 2012. CoIPs were performed in transiently transfected or stable HEK293T cells.…”

Section: Total Cell Lysates and Co-immunoprecipitationmentioning

confidence: 99%

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Cortactin is a scaffolding platform for the E-Cadherin adhesion complex controlled by protein kinase D1 phosphorylation

Sroka

Lint

Katz

et al. 2016

Journal of Cell Science

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Dynamic regulation of cell-cell adhesion by the coordinated formation and dissolution of E-cadherin-based adherens junctions is crucial for tissue homeostasis. The actin-binding protein cortactin interacts with E-cadherin and enables F-actin accumulation at adherens junctions. Here, we were interested to study the broader functional interactions of cortactin in adhesion complexes. In line with literature, we demonstrate that cortactin binds to E-cadherin, and that a posttranslational modification of cortactin, RhoA-induced phosphorylation by protein kinase D1 (PKD1; also known as PRKD1) at S298, impairs adherens junction assembly and supports their dissolution. Two new S298-phosphorylation-dependent interactions were also identified, namely, that phosphorylation of cortactin decreases its interaction with β-catenin and the actin-binding protein vinculin. In addition, binding of vinculin to β-catenin, as well as linkage of vinculin to F-actin, are also significantly compromised upon phosphorylation of cortactin. Accordingly, we found that regulation of cell-cell adhesion by phosphorylation of cortactin downstream of RhoA and PKD1 is vitally dependent on vinculin-mediated protein interactions. Thus, cortactin, unexpectedly, is an important integration node for the dynamic regulation of protein complexes during breakdown and formation of adherens junctions.

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Section: Methodsmentioning

confidence: 99%

Section: Intestinal Permeability Assaymentioning

confidence: 99%

Section: Intestinal Permeability Assaymentioning

confidence: 99%

Section: Intestinal Permeability Assaymentioning

confidence: 99%

Section: Total Cell Lysates and Co-immunoprecipitationmentioning

confidence: 99%

See 3 more Smart Citations

Cortactin is a scaffolding platform for the E-Cadherin adhesion complex controlled by protein kinase D1 phosphorylation

Sroka

Lint

Katz

et al. 2016

Journal of Cell Science

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Polyphenols from brown alga, Padina boergesenii (Allendar & Kraft) decelerates renal cancer growth involving cell cycle arrest and induction of apoptosis in renal carcinoma cells

Karthikeyan

Thirugnanasambandan

2018

Environmental Toxicology

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In our previous work, we assessed the ameliorative effect of crude extract from Padina boergesenii. In this report, we have extended these study by fractionating the methanol extract with methanol:ethylacetate (1:3,v/v) (MME-F) and assessed the cytotoxic effect of MME-F fraction in human renal carcinoma cell lines (A498 and ACHN). The fraction had time-and dose-dependent inhibition of cancer cell proliferation, migration with deceleration of cancer growth at EC -22.73 μg in A498 and 26.43 μg in ACHN cells. Cells treated at EC value 25 μg displayed twofold greater ability to induce early and late stage of apoptosis. The cells treated with polyphenolic fraction (MME-F) induced cell cycle arrest at G2/M phase. HPLC/DAD chromatographic procedures quantified polyphenols from active fraction (MME-F). These data revealed the functional activity of polyphenols from brown alga, P. boergesenii as a potent inhibitor of cancer proliferation with induction of apoptosis, it suggest their applicability in preventing cancer metastasis.

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PKD1 Phosphorylation-Dependent Degradation of SNAIL by SCF-FBXO11 Regulates Epithelial-Mesenchymal Transition and Metastasis

et al. 2014

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SUMMARY Metastatic dissemination is often initiated by the reactivation of an embryonic development program referred to as epithelial-mesenchymal transition (EMT). The transcription factor SNAIL promotes EMT and elicits associated pathological characteristics, such as invasion, metastasis and stemness. To better understand the post-translational regulation of SNAIL, we performed a luciferase-based genome-wide E3 ligase siRNA library screen and identified SCF-FBXO11 as an important E3 which targets SNAIL for ubiquitylation and degradation. Furthermore, we discovered that SNAIL degradation by FBXO11 is dependent on Serine-11 phosphorylation of SNAIL by protein kinase D1 (PKD1). FBXO11 blocks SNAIL-induced EMT, tumor initiation and metastasis in multiple breast cancer models. These findings establish the PKD1-FBXO11-SNAIL axis as a mechanism of post-translational regulation of EMT and cancer metastasis.

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Protein Kinase D1 Mediates Anchorage-dependent and -independent Growth of Tumor Cells via the Zinc Finger Transcription Factor Snail1

Cited by 35 publications

References 37 publications

Cortactin is a scaffolding platform for the E-Cadherin adhesion complex controlled by protein kinase D1 phosphorylation

Cortactin is a scaffolding platform for the E-Cadherin adhesion complex controlled by protein kinase D1 phosphorylation

Polyphenols from brown alga, Padina boergesenii (Allendar & Kraft) decelerates renal cancer growth involving cell cycle arrest and induction of apoptosis in renal carcinoma cells

PKD1 Phosphorylation-Dependent Degradation of SNAIL by SCF-FBXO11 Regulates Epithelial-Mesenchymal Transition and Metastasis

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