NDLI: Death-effector Filaments: Novel Cytoplasmic Structures that Recruit Caspases and Trigger Apoptosis

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Death-effector Filaments: Novel Cytoplasmic Structures that Recruit Caspases and Trigger Apoptosis

Content Provider	Semantic Scholar
Author	Siegel, Richard M. Zheng, Lixin Ng, Samuel Yao-Ming Bertin, John Lenardo, Michael J.
Copyright Year	1998
Abstract	The death-effector domain (DED) is a critical protein interaction domain that recruits caspases into complexes with members of the TNF-receptor superfamily. Apoptosis can also be induced by expressing certain DED-containing proteins without surface receptor cross-linking. Using Green Fluorescent Protein to examine DED-containing proteins in living cells, we show that these proteins cause apoptosis by forming novel cytoplasmic filaments that recruit and activate pro-caspase zymogens. Formation of these filaments, which we term death-effector filaments, was blocked by coexpression of viral antiapoptotic DED-containing proteins, but not by bcl-2 family proteins. Thus, formation of death-effector filaments allows a regulated intracellular assembly of apoptosis-signaling complexes that can initiate or amplify apoptotic stimuli independently of receptors at the plasma membrane.
Starting Page	1243
Ending Page	1253
Page Count	11
File Format	PDF HTM / HTML
PubMed reference number	9606215v1
Volume Number	141
Journal	The Journal of cell biology
Alternate Webpage(s)	http://jcb.rupress.org/content/jcb/141/5/1243.full.pdf
Alternate Webpage(s)	http://ftp.ncbi.nlm.nih.gov/pub/pmc/be/d5/9802036.PMC2137190.pdf
Language	English
Access Restriction	Open
Subject Keyword	Activation action Antiapoptotic Agent Antineutrophil Cytoplasmic Antibodies Apoptosis BCL2 gene Enzyme Precursors Plasma membrane caspase protein protein interaction
Content Type	Text
Resource Type	Article

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