Dissection of DIAP1 functional domains via a mutant replacement strategy. (Q52651094)

5 May 2018

title

Dissection of DIAP1 functional domains via a mutant replacement strategy. (English)

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5 May 2018

author name string

Takakazu Yokokura

1

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5 May 2018

Doug Dresnek

2

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5 May 2018

Neda Huseinovic

3

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5 May 2018

Simonetta Lisi

4

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5 May 2018

Eltyeb Abdelwahid

5

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5 May 2018

Peter Bangs

6

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5 May 2018

Kristin White

7

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5 May 2018

language of work or name

English

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publication date

15 September 2004

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5 May 2018

Journal of Biological Chemistry

published in

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5 May 2018

volume

279

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5 May 2018

page(s)

52603-52612

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5 May 2018

issue

50

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5 May 2018

IAP proteins: blocking the road to death's door

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X-linked IAP is a direct inhibitor of cell-death proteases

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Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination

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Molecular mechanisms of DrICE inhibition by DIAP1 and removal of inhibition by Reaper, Hid and Grim.

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The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID.

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Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM.

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Structural and biochemical basis of apoptotic activation by Smac/DIABLO

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Structural basis of IAP recognition by Smac/DIABLO

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Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain

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The damage-responsive Drosophila gene sickle encodes a novel IAP binding protein similar to but distinct from reaper, grim, and hid.

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sickle, a novel Drosophila death gene in the reaper/hid/grim region, encodes an IAP-inhibitory protein

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Drosophila sickle is a novel grim-reaper cell death activator

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Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

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HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins

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Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins

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The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity

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The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif

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A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death

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The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis.

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Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death

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Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function

21 January 2018

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Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms.

21 January 2018

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Morgue mediates apoptosis in the Drosophila melanogaster retina by promoting degradation of DIAP1.

21 January 2018

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Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1.

21 January 2018

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Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition

21 January 2018

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Drosophila Morgue is an F box/ubiquitin conjugase domain protein important for grim-reaper mediated apoptosis.

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Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis.

21 January 2018

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Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro

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Reaper is regulated by IAP-mediated ubiquitination.

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Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death

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The head involution defective gene of Drosophila melanogaster functions in programmed cell death.

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Cell killing by the Drosophila gene reaper.

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salvador Promotes both cell cycle exit and apoptosis in Drosophila and is mutated in human cancer cell lines

21 January 2018

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Regulators of IAP function: coming to grips with the grim reaper

21 January 2018

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The Drosophila caspase DRONC is regulated by DIAP1

21 January 2018

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The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC.

21 January 2018

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IAP-antagonists exhibit non-redundant modes of action through differential DIAP1 binding

21 January 2018

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The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM.

21 January 2018

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Biochemical and genetic interactions between Drosophila caspases and the proapoptotic genes rpr, hid, and grim

21 January 2018

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Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells

21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M409691200

1 reference

5 May 2018

PubMed ID

15371434

1 reference

5 May 2018