P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.

Fas-associated death domain (DD) adaptor (FADD), a member of the DD superfamily, contains both a DD and a death effector domain (DED) that are important in mediating FAS ligand-induced apoptotic signaling. P45 is a unique member of the DD superfamily in that it has a domain with sequence and structu...

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Main Authors: Tsung-Chang Sung, Zhijiang Chen, Sandrine Thuret, Marçal Vilar, Fred H Gage, Roland Riek, Kuo-Fen Lee
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3720591?pdf=render
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author Tsung-Chang Sung
Zhijiang Chen
Sandrine Thuret
Marçal Vilar
Fred H Gage
Roland Riek
Kuo-Fen Lee
author_facet Tsung-Chang Sung
Zhijiang Chen
Sandrine Thuret
Marçal Vilar
Fred H Gage
Roland Riek
Kuo-Fen Lee
author_sort Tsung-Chang Sung
collection DOAJ
description Fas-associated death domain (DD) adaptor (FADD), a member of the DD superfamily, contains both a DD and a death effector domain (DED) that are important in mediating FAS ligand-induced apoptotic signaling. P45 is a unique member of the DD superfamily in that it has a domain with sequence and structural characteristics of both DD and DED. We show that p45 forms a complex with FADD and diminishes Fas-FADD mediated death signaling. The DED of FADD is required for the complex formation with p45. Following spinal cord injury, transgenic mice over-expressing p45 exhibit increased neuronal survival, decreased retraction of corticospinal tract fibers and improved functional recovery. Understanding p45-mediated cellular and molecular mechanisms may provide insights into facilitating nerve regeneration in humans.
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spelling doaj.art-892cb4cac9974abdb6bb42f526d6949d2022-12-21T23:21:15ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0187e6928610.1371/journal.pone.0069286P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.Tsung-Chang SungZhijiang ChenSandrine ThuretMarçal VilarFred H GageRoland RiekKuo-Fen LeeFas-associated death domain (DD) adaptor (FADD), a member of the DD superfamily, contains both a DD and a death effector domain (DED) that are important in mediating FAS ligand-induced apoptotic signaling. P45 is a unique member of the DD superfamily in that it has a domain with sequence and structural characteristics of both DD and DED. We show that p45 forms a complex with FADD and diminishes Fas-FADD mediated death signaling. The DED of FADD is required for the complex formation with p45. Following spinal cord injury, transgenic mice over-expressing p45 exhibit increased neuronal survival, decreased retraction of corticospinal tract fibers and improved functional recovery. Understanding p45-mediated cellular and molecular mechanisms may provide insights into facilitating nerve regeneration in humans.http://europepmc.org/articles/PMC3720591?pdf=render
spellingShingle Tsung-Chang Sung
Zhijiang Chen
Sandrine Thuret
Marçal Vilar
Fred H Gage
Roland Riek
Kuo-Fen Lee
P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.
PLoS ONE
title P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.
title_full P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.
title_fullStr P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.
title_full_unstemmed P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.
title_short P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.
title_sort p45 forms a complex with fadd and promotes neuronal cell survival following spinal cord injury
url http://europepmc.org/articles/PMC3720591?pdf=render
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