International Journal of Research and Engineering (IJRE)

The Editor-In-Chief (EIC) for the International Journal of Research in Science

The Editor-In-Chief

Klonetics Plant Science Inc.

Consultant

Amr worked at Klonetics Plant Science Inc. as a Consultant

University of Saskatchewan

Postdoctoral Research Fellow

Amr worked at University of Saskatchewan as a Postdoctoral Research Fellow

University of Saskatchewan

Research associate at College of Medicine

Amr worked at University of Saskatchewan as a Research associate at College of Medicine

University of Saskatchewan

Sessional Lecturer

Amr worked at University of Saskatchewan as a Sessional Lecturer

Avitas Pharmakos Company for medical marijuana

Chief Science officer at Avitas Pharmakos Company (Avitas) Cannabis company

Amr worked at Avitas Pharmakos Company for medical marijuana as a Chief Science officer at Avitas Pharmakos Company (Avitas) Cannabis company

Faculty of Science, Egypt

Faculty member

Amr worked at Faculty of Science, Egypt as a Faculty member

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis

Cell Reports

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis

Cell Reports

FRIENDLY Regulates Mitochondrial Distribution, Fusion, and Quality Control in Arabidopsis

Plant Physiology

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis

Cell Reports

FRIENDLY Regulates Mitochondrial Distribution, Fusion, and Quality Control in Arabidopsis

Plant Physiology

Imaging and analysis of mitochondrial dynamics in living cells

Methods in Molecular Biology 1305

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis

Cell Reports

FRIENDLY Regulates Mitochondrial Distribution, Fusion, and Quality Control in Arabidopsis

Plant Physiology

Imaging and analysis of mitochondrial dynamics in living cells

Methods in Molecular Biology 1305

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis

Cell Reports

FRIENDLY Regulates Mitochondrial Distribution, Fusion, and Quality Control in Arabidopsis

Plant Physiology

Imaging and analysis of mitochondrial dynamics in living cells

Methods in Molecular Biology 1305

The intrinsically kinase-inactive EPHB6 receptor predisposes cancer cells to DR5-induced apoptosis by promoting mitochondrial fragmentation.

Oncotarget

Death Receptor 5 (DR5) is a promising target for cancer therapy due to its ability to selectively induce apoptosis in cancer cells. However, the therapeutic usefulness of DR5 agonists is currently limited by the frequent resistance of malignant tumours to its activation. The identification of molecular mechanisms that determine outcomes of DR5 action is therefore crucial for improving the efficiency of DR5-activating reagents in cancer treatment. Here, we provide evidence that an intrinsically kinase-inactive member of the Eph group of receptor tyrosine kinases, EPHB6, induces marked fragmentation of the mitochondrial network in breast cancer cells of triple-negative origin, lacking expression of the estrogen, progesterone and HER2 receptors. Remarkably, this response renders cancer cells more susceptible to DR5-mediated apoptosis. EPHB6 action in mitochondrial fragmentation proved to depend on its ability to activate the ERK-DRP1 pathway, which increases the frequency of organelle fission. Moreover, DRP1 activity is also essential to the EPHB6-mediated pro-apoptotic response that we observe in the context of DR5 activation. These findings provide the first description of a member of the receptor tyrosine kinase family capable of producing a pro-apoptotic effect through the activation of ERK-DRP1 signaling and subsequent mitochondrial fragmentation. Our observations are of potential practical importance, as they imply that DR5-activating therapeutic approaches should be applied in a more personalized manner to primarily treat EPHB6-expressing tumours. Finally, our findings also suggest that the EPHB6 receptor itself may represent a promising target for cancer therapy, since EPHB6 and DR5 co-activation should support more efficient elimination of cancer cells.

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis

Cell Reports

FRIENDLY Regulates Mitochondrial Distribution, Fusion, and Quality Control in Arabidopsis

Plant Physiology

Imaging and analysis of mitochondrial dynamics in living cells

Methods in Molecular Biology 1305

The intrinsically kinase-inactive EPHB6 receptor predisposes cancer cells to DR5-induced apoptosis by promoting mitochondrial fragmentation.

Oncotarget

Death Receptor 5 (DR5) is a promising target for cancer therapy due to its ability to selectively induce apoptosis in cancer cells. However, the therapeutic usefulness of DR5 agonists is currently limited by the frequent resistance of malignant tumours to its activation. The identification of molecular mechanisms that determine outcomes of DR5 action is therefore crucial for improving the efficiency of DR5-activating reagents in cancer treatment. Here, we provide evidence that an intrinsically kinase-inactive member of the Eph group of receptor tyrosine kinases, EPHB6, induces marked fragmentation of the mitochondrial network in breast cancer cells of triple-negative origin, lacking expression of the estrogen, progesterone and HER2 receptors. Remarkably, this response renders cancer cells more susceptible to DR5-mediated apoptosis. EPHB6 action in mitochondrial fragmentation proved to depend on its ability to activate the ERK-DRP1 pathway, which increases the frequency of organelle fission. Moreover, DRP1 activity is also essential to the EPHB6-mediated pro-apoptotic response that we observe in the context of DR5 activation. These findings provide the first description of a member of the receptor tyrosine kinase family capable of producing a pro-apoptotic effect through the activation of ERK-DRP1 signaling and subsequent mitochondrial fragmentation. Our observations are of potential practical importance, as they imply that DR5-activating therapeutic approaches should be applied in a more personalized manner to primarily treat EPHB6-expressing tumours. Finally, our findings also suggest that the EPHB6 receptor itself may represent a promising target for cancer therapy, since EPHB6 and DR5 co-activation should support more efficient elimination of cancer cells.

EPHB6 augments both development and drug sensitivity of triple-negative breast cancer tumours.

Oncogene

Therapeutic relevance of the protein phosphatase 2A in cancer

Oncotarget

The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis

Cell Reports

FRIENDLY Regulates Mitochondrial Distribution, Fusion, and Quality Control in Arabidopsis

Plant Physiology

Imaging and analysis of mitochondrial dynamics in living cells

Methods in Molecular Biology 1305

The intrinsically kinase-inactive EPHB6 receptor predisposes cancer cells to DR5-induced apoptosis by promoting mitochondrial fragmentation.

Oncotarget

Death Receptor 5 (DR5) is a promising target for cancer therapy due to its ability to selectively induce apoptosis in cancer cells. However, the therapeutic usefulness of DR5 agonists is currently limited by the frequent resistance of malignant tumours to its activation. The identification of molecular mechanisms that determine outcomes of DR5 action is therefore crucial for improving the efficiency of DR5-activating reagents in cancer treatment. Here, we provide evidence that an intrinsically kinase-inactive member of the Eph group of receptor tyrosine kinases, EPHB6, induces marked fragmentation of the mitochondrial network in breast cancer cells of triple-negative origin, lacking expression of the estrogen, progesterone and HER2 receptors. Remarkably, this response renders cancer cells more susceptible to DR5-mediated apoptosis. EPHB6 action in mitochondrial fragmentation proved to depend on its ability to activate the ERK-DRP1 pathway, which increases the frequency of organelle fission. Moreover, DRP1 activity is also essential to the EPHB6-mediated pro-apoptotic response that we observe in the context of DR5 activation. These findings provide the first description of a member of the receptor tyrosine kinase family capable of producing a pro-apoptotic effect through the activation of ERK-DRP1 signaling and subsequent mitochondrial fragmentation. Our observations are of potential practical importance, as they imply that DR5-activating therapeutic approaches should be applied in a more personalized manner to primarily treat EPHB6-expressing tumours. Finally, our findings also suggest that the EPHB6 receptor itself may represent a promising target for cancer therapy, since EPHB6 and DR5 co-activation should support more efficient elimination of cancer cells.

EPHB6 augments both development and drug sensitivity of triple-negative breast cancer tumours.

Oncogene

Ligand stimulation induces clathrin- and Rab5- dependent downregulation of the kinase-dead EphB6 receptor preceded by the disruption of EphB6-Hsp90 interaction

Cellular Signalling