DEDD regulates degradation of intermediate filaments during apoptosis (Q24673637)

1

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Olaf Schickling

2

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Alexander H Stegh

3

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Robert G Oshima

4

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David Dinsdale

5

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Marcus E Peter

Identification and characterization of DEDD2, a death effector domain-containing protein

7

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language of work or name

English

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publication date

16 September 2002

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published in

Journal of Cell Biology

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volume

158

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issue

6

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page(s)

1051-66

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cites work

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Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis

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DEDD, a novel death effector domain-containing protein, targeted to the nucleolus

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Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis

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Lamin proteolysis facilitates nuclear events during apoptosis

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Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC

7 April 2017

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Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation

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Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis

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Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl-2 action

7 April 2017

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Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis

7 April 2017

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Protein regulation by monoubiquitin

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Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis

7 April 2017

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Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain

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Cell death: the significance of apoptosis

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Apoptosis and keratin intermediate filaments

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Apoptosis and caspases

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Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription

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Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis

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The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm.

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Active caspases and cleaved cytokeratins are sequestered into cytoplasmic inclusions in TRAIL-induced apoptosis

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Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis

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Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal

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28 September 2017

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Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targeting modulation

28 September 2017

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Apoptosis generates stable fragments of human type I keratins

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PubMed

https://pubmed.ncbi.nlm.nih.gov/12235123

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Apoptosis-associated proteolysis of vimentin in human prostate epithelial tumor cells

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12235123