Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination (Q27642254)

Death-associated inhibitor of apoptosis 1 Dmel_CG12284

GOA release 2020-03-11

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Head involution defective Dmel_CG5123

GOA release 2020-03-11

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GOA release 2020-03-11

protein ubiquitination

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2

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Yigong Shi

7

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Jun R Huh

3

object named as

Jun R Huh

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author name string

Jijie Chai

1

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Jia-Wei Wu

4

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Wenyu Li

5

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Bruce A Hay

Nature structural biology

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publication date

November 2003

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published in

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volume

10

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issue

11

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page(s)

892-8

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cites work

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An essential role for the caspase dronc in developmentally programmed cell death in Drosophila.

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IAP family proteins--suppressors of apoptosis

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IAP proteins: blocking the road to death's door

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Understanding IAP function and regulation: a view from Drosophila

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

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

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

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Structural and biochemical basis of apoptotic activation by Smac/DIABLO

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Mechanism of XIAP-mediated inhibition of caspase-9

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A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis

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Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator

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HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis

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Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway

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Unrestrained caspase-dependent cell death caused by loss of Diap1 function requires the Drosophila Apaf-1 homolog, Dark

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The role of ARK in stress-induced apoptosis in Drosophila cells

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

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

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1 reference

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

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

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

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

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

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

21 January 2018

1 reference

Jafrac2 is an IAP antagonist that promotes cell death by liberating Dronc from DIAP1

21 January 2018

1 reference

The Drosophila caspase DRONC is regulated by DIAP1

21 January 2018

1 reference

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

21 January 2018

1 reference

Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides

21 January 2018

1 reference

Structural basis of IAP recognition by Smac/DIABLO

21 January 2018

1 reference

Regulation of the Apaf-1/caspase-9 apoptosome by caspase-3 and XIAP.

21 January 2018

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Processing of X-ray diffraction data collected in oscillation mode

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AMoRe: an automated package for molecular replacement

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Improved methods for building protein models in electron density maps and the location of errors in these models

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

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

21 January 2018

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A conserved tetrapeptide motif: potentiating apoptosis through IAP-binding

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