Protein phosphatase 1-dependent dephosphorylation of Akt is the prime signaling event in sphingosine-induced apoptosis in Jurkat cells. (Q54614020)

1 June 2018

title

Protein phosphatase 1-dependent dephosphorylation of Akt is the prime signaling event in sphingosine-induced apoptosis in Jurkat cells. (English)

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author name string

Faisal Thayyullathil

1

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Shahanas Chathoth

2

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Allen Shahin

3

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Jaleel Kizhakkayil

4

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Abdulkader Hago

5

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Mahendra Patel

6

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Sehamuddin Galadari

7

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publication date

1 April 2011

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Journal of Cellular Biochemistry

published in

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volume

112

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issue

4

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page(s)

1138-1153

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Inhibition of the insulin receptor tyrosine kinase by sphingosine

cites work

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One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis.

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Protein phosphatase 1alpha is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis

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Long chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid

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Role of AKT kinase in sphingosine-induced apoptosis in human hepatoma cells

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Histone acetylation-independent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes

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Sphingosine in apoptosis signaling

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Mechanisms and Functions of Cell Death

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Activation of caspase-3-like proteases in apoptosis induced by sphingosine and other long-chain bases in Hep3B hepatoma cells

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Characterization of the interleukin-1beta-converting enzyme/ced-3-family protease, caspase-3/CPP32, in Hodgkin's disease: lack of caspase-3 expression in nodular lymphocyte predominance Hodgkin's disease

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Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1

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Phosphatidic acid is a potent and selective inhibitor of protein phosphatase 1 and an inhibitor of ceramide-mediated responses

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Inhibitory phosphorylation of PP1alpha catalytic subunit during the G(1)/S transition

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A novel immunosuppressive agent FTY720 induced Akt dephosphorylation in leukemia cells

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Inactivation and dephosphorylation of protein kinase Balpha (PKBalpha) promoted by hyperosmotic stress

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Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473.

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Prevention of docosahexaenoic acid-induced cytotoxicity by phosphatidic acid in Jurkat leukemic cells: the role of protein phosphatase-1.

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Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase

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Rapid reactive oxygen species (ROS) generation induced by curcumin leads to caspase-dependent and -independent apoptosis in L929 cells.

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Protein phosphatase 1alpha-mediated stimulation of apoptosis is associated with dephosphorylation of the retinoblastoma protein

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Prognostic significance of activated Akt expression in pancreatic ductal adenocarcinoma

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Activation of p38 mitogen-activated protein kinase is required for death receptor-independent caspase-8 activation and cell death in response to sphingosine

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HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation

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Identifiers

DOI

10.1002/JCB.23033

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