Tyrosine 311 is phosphorylated by c-Abl and promotes the apoptotic effect of PKCδ in glioma cells

Wei Lu; Susan Finnis; Cunli Xiang; Hae Kyung Lee; Yael Markowitz; Hana Okhrimenko; Chaya Brodie

doi:10.1016/j.bbrc.2006.11.028

Tyrosine 311 is phosphorylated by c-Abl and promotes the apoptotic effect of PKCδ in glioma cells

Wei Lu, Susan Finnis, Cunli Xiang, Hae Kyung Lee, Yael Markowitz, Hana Okhrimenko, Chaya Brodie

The Mina and Everard Goodman Faculty of Life Sciences

Research output: Contribution to journal › Article › peer-review

27 Scopus citations

Abstract

In this study we characterized the phosphorylation of tyrosine 311 and its role in the apoptotic function of PKCδ in glioma cells. We found that c-Abl phosphorylated PKCδ on tyrosine 311 in response to H₂O₂ and that this phosphorylation contributed to the apoptotic effect of H₂O₂. In contrast, Src, Lyn, and Yes were not involved in the phosphorylation of tyrosine 311 by H₂O₂. A phosphomimetic PKCδ mutant, in which tyrosine 311 was mutated to glutamic acid (PKCδY311E), induced a large degree of cell apoptosis. Overexpression of the PKCδY311E mutant induced the phosphorylation of p38 and inhibition of p38 abolished the apoptotic effect of the PKCδ mutant. These results suggest an important role of tyrosine 311 in the apoptotic function of PKCδ and implicate c-Abl as the kinase that phosphorylates this tyrosine.

Original language	English
Pages (from-to)	431-436
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	352
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2006.11.028
State	Published - 12 Jan 2007

Bibliographical note

Funding Information:
This work was supported by NIH Grant RO1CA109196 and by the William and Karen Davidson Fund, Hermelin Brain Tumor Center.

Funding

This work was supported by NIH Grant RO1CA109196 and by the William and Karen Davidson Fund, Hermelin Brain Tumor Center.

Funders	Funder number
Hermelin Brain Tumor Center
William and Karen Davidson Fund
National Institutes of Health
National Cancer Institute	R01CA109196

Keywords

Apoptosis
Glioma
HO
PKCδ
Src
Tyrosine phosphorylation
c-Abl

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10.1016/j.bbrc.2006.11.028

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title = "Tyrosine 311 is phosphorylated by c-Abl and promotes the apoptotic effect of PKCδ in glioma cells",

abstract = "In this study we characterized the phosphorylation of tyrosine 311 and its role in the apoptotic function of PKCδ in glioma cells. We found that c-Abl phosphorylated PKCδ on tyrosine 311 in response to H2O2 and that this phosphorylation contributed to the apoptotic effect of H2O2. In contrast, Src, Lyn, and Yes were not involved in the phosphorylation of tyrosine 311 by H2O2. A phosphomimetic PKCδ mutant, in which tyrosine 311 was mutated to glutamic acid (PKCδY311E), induced a large degree of cell apoptosis. Overexpression of the PKCδY311E mutant induced the phosphorylation of p38 and inhibition of p38 abolished the apoptotic effect of the PKCδ mutant. These results suggest an important role of tyrosine 311 in the apoptotic function of PKCδ and implicate c-Abl as the kinase that phosphorylates this tyrosine.",

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author = "Wei Lu and Susan Finnis and Cunli Xiang and Lee, {Hae Kyung} and Yael Markowitz and Hana Okhrimenko and Chaya Brodie",

note = "Funding Information: This work was supported by NIH Grant RO1CA109196 and by the William and Karen Davidson Fund, Hermelin Brain Tumor Center.",

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AU - Lu, Wei

AU - Finnis, Susan

AU - Xiang, Cunli

AU - Lee, Hae Kyung

AU - Markowitz, Yael

AU - Okhrimenko, Hana

AU - Brodie, Chaya

N1 - Funding Information: This work was supported by NIH Grant RO1CA109196 and by the William and Karen Davidson Fund, Hermelin Brain Tumor Center.

PY - 2007/1/12

Y1 - 2007/1/12

N2 - In this study we characterized the phosphorylation of tyrosine 311 and its role in the apoptotic function of PKCδ in glioma cells. We found that c-Abl phosphorylated PKCδ on tyrosine 311 in response to H2O2 and that this phosphorylation contributed to the apoptotic effect of H2O2. In contrast, Src, Lyn, and Yes were not involved in the phosphorylation of tyrosine 311 by H2O2. A phosphomimetic PKCδ mutant, in which tyrosine 311 was mutated to glutamic acid (PKCδY311E), induced a large degree of cell apoptosis. Overexpression of the PKCδY311E mutant induced the phosphorylation of p38 and inhibition of p38 abolished the apoptotic effect of the PKCδ mutant. These results suggest an important role of tyrosine 311 in the apoptotic function of PKCδ and implicate c-Abl as the kinase that phosphorylates this tyrosine.

AB - In this study we characterized the phosphorylation of tyrosine 311 and its role in the apoptotic function of PKCδ in glioma cells. We found that c-Abl phosphorylated PKCδ on tyrosine 311 in response to H2O2 and that this phosphorylation contributed to the apoptotic effect of H2O2. In contrast, Src, Lyn, and Yes were not involved in the phosphorylation of tyrosine 311 by H2O2. A phosphomimetic PKCδ mutant, in which tyrosine 311 was mutated to glutamic acid (PKCδY311E), induced a large degree of cell apoptosis. Overexpression of the PKCδY311E mutant induced the phosphorylation of p38 and inhibition of p38 abolished the apoptotic effect of the PKCδ mutant. These results suggest an important role of tyrosine 311 in the apoptotic function of PKCδ and implicate c-Abl as the kinase that phosphorylates this tyrosine.

KW - Apoptosis

KW - Glioma

KW - HO

KW - PKCδ

KW - Src

KW - Tyrosine phosphorylation

KW - c-Abl

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Tyrosine 311 is phosphorylated by c-Abl and promotes the apoptotic effect of PKCδ in glioma cells

Abstract

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Keywords

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