Nonapoptotic functions of FADD-binding death receptors and their signaling molecules

Sun Mi Park; Robert Schickel; Marcus E. Peter

doi:10.1016/j.ceb.2005.09.010

Nonapoptotic functions of FADD-binding death receptors and their signaling molecules

Sun Mi Park, Robert Schickel, Marcus E. Peter^*

^*Corresponding author for this work

Medicine, Hematology Oncology Division

Research output: Contribution to journal › Review article › peer-review

121 Scopus citations

Abstract

Death receptors (DRs) are surface receptors that when triggered have the capacity to induce apoptosis in cells by forming the death-inducing signaling complex (DISC). The first protein recruited to form the DISC is the adaptor protein FADD/Mort1. Some members of the DR family, CD95 and the TRAIL receptors DR4 and DR5, directly bind FADD, whereas others, such as TNF receptor I and DR3, initially bind another adaptor protein, TRADD, which then recruits FADD. While all DRs can activate both apoptotic and non-apoptotic pathways, it has been widely assumed that the main physiological role of FADD-binding death receptors is to trigger apoptosis. However, recent work has ascribed multiple non-apoptotic activities to these receptors and/or the signaling components of the DISC.

Original language	English (US)
Pages (from-to)	610-616
Number of pages	7
Journal	Current Opinion in Cell Biology
Volume	17
Issue number	6
DOIs	https://doi.org/10.1016/j.ceb.2005.09.010
State	Published - Dec 2005

Funding

We would like to apologize to all the colleagues whose work could not be cited due to space limitations. Support to ME Peter has been provided by the National Institute of Health grants GM61712 and CA95319. R Schickel is supported by the Department of Defense fellowship DAMD17-03-1-0200.

ASJC Scopus subject areas

Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.ceb.2005.09.010

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title = "Nonapoptotic functions of FADD-binding death receptors and their signaling molecules",

abstract = "Death receptors (DRs) are surface receptors that when triggered have the capacity to induce apoptosis in cells by forming the death-inducing signaling complex (DISC). The first protein recruited to form the DISC is the adaptor protein FADD/Mort1. Some members of the DR family, CD95 and the TRAIL receptors DR4 and DR5, directly bind FADD, whereas others, such as TNF receptor I and DR3, initially bind another adaptor protein, TRADD, which then recruits FADD. While all DRs can activate both apoptotic and non-apoptotic pathways, it has been widely assumed that the main physiological role of FADD-binding death receptors is to trigger apoptosis. However, recent work has ascribed multiple non-apoptotic activities to these receptors and/or the signaling components of the DISC.",

author = "Park, {Sun Mi} and Robert Schickel and Peter, {Marcus E.}",

note = "Funding Information: We would like to apologize to all the colleagues whose work could not be cited due to space limitations. Support to ME Peter has been provided by the National Institute of Health grants GM61712 and CA95319. R Schickel is supported by the Department of Defense fellowship DAMD17-03-1-0200.",

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AU - Schickel, Robert

AU - Peter, Marcus E.

N1 - Funding Information: We would like to apologize to all the colleagues whose work could not be cited due to space limitations. Support to ME Peter has been provided by the National Institute of Health grants GM61712 and CA95319. R Schickel is supported by the Department of Defense fellowship DAMD17-03-1-0200.

PY - 2005/12

Y1 - 2005/12

N2 - Death receptors (DRs) are surface receptors that when triggered have the capacity to induce apoptosis in cells by forming the death-inducing signaling complex (DISC). The first protein recruited to form the DISC is the adaptor protein FADD/Mort1. Some members of the DR family, CD95 and the TRAIL receptors DR4 and DR5, directly bind FADD, whereas others, such as TNF receptor I and DR3, initially bind another adaptor protein, TRADD, which then recruits FADD. While all DRs can activate both apoptotic and non-apoptotic pathways, it has been widely assumed that the main physiological role of FADD-binding death receptors is to trigger apoptosis. However, recent work has ascribed multiple non-apoptotic activities to these receptors and/or the signaling components of the DISC.

AB - Death receptors (DRs) are surface receptors that when triggered have the capacity to induce apoptosis in cells by forming the death-inducing signaling complex (DISC). The first protein recruited to form the DISC is the adaptor protein FADD/Mort1. Some members of the DR family, CD95 and the TRAIL receptors DR4 and DR5, directly bind FADD, whereas others, such as TNF receptor I and DR3, initially bind another adaptor protein, TRADD, which then recruits FADD. While all DRs can activate both apoptotic and non-apoptotic pathways, it has been widely assumed that the main physiological role of FADD-binding death receptors is to trigger apoptosis. However, recent work has ascribed multiple non-apoptotic activities to these receptors and/or the signaling components of the DISC.

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Nonapoptotic functions of FADD-binding death receptors and their signaling molecules

Abstract

Funding

ASJC Scopus subject areas

UN SDGs

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