FLIP and the death effector domain family (Q28297969)

Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities

Europe PubMed Central

title

FLIP and the death effector domain family (English)

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author name string

J W Yu

series ordinal

1

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Y Shi

series ordinal

2

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language of work or name

English

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publication date

20 October 2008

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published in

Oncogene

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volume

27

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issue

48

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page(s)

6216-27

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cites work

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Caspase activation is required for T cell proliferation

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FLIP switches Fas-mediated glucose signaling in human pancreatic beta cells from apoptosis to cell replication

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Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis

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Ligand-independent redistribution of Fas (CD95) into lipid rafts mediates clonotypic T cell death.

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Cellular FLIP inhibits beta-catenin ubiquitylation and enhances Wnt signaling.

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Viral FLIP enhances Wnt signaling downstream of stabilized beta-catenin, leading to control of cell growth

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FADD self-association is required for stable interaction with an activated death receptor

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Fas engagement induces neurite growth through ERK activation and p35 upregulation

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Fas engagement accelerates liver regeneration after partial hepatectomy

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A matter of life and death

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Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling

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Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling

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The CD95 Receptor: Apoptosis Revisited

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