Induction of apoptosis by p110C requires mitochondrial translocation of the proapoptotic BCL-2 family member BAD (Q24301096)

2

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Qing Sun

3

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Luyang Yao

4

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Yongzhi Jian

5

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Jieqiong Lu

6

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Jianxin Gu

Programmed cell death in animal development

7

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language of work or name

English

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publication date

6 February 2006

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published in

FEBS Letters

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volume

580

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issue

3

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page(s)

813-21

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cites work

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Bcl-2 family proteins

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Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

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p21-activated kinase 1 phosphorylates the death agonist bad and protects cells from apoptosis

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p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD

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Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155.

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Mitochondria and apoptosis

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Different effects of p58PITSLRE on the apoptosis induced by etoposide, cycloheximide and serum-withdrawal in human hepatocarcinoma cells

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The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis

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Serum bioactive lysophospholipids prevent TRAIL-induced apoptosis via PI3K/Akt-dependent cFLIP expression and Bad phosphorylation

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Mechanism of activation of protein kinase B by insulin and IGF-1

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Checkpoints of dueling dimers foil death wishes

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Apoptosis meets signal transduction: elimination of a BAD influence

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Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A

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Tumor necrosis factor induces phosphorylation and translocation of BAD through a phosphatidylinositide-3-OH kinase-dependent pathway

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Fas-induced apoptosis in human malignant melanoma cell lines is associated with the activation of the p34(cdc2)-related PITSLRE protein kinases

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PITSLRE protein kinase activity is associated with apoptosis

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