P45 forms a complex with FADD and promotes neuronal cell survival following spinal cord injury.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 23935974.
- Also identified by DOI 10.1371/journal.pone.0069286 and PMC identifier 3720591.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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.
Medical subject headings
- Fas-Associated Death Domain Protein
- Membrane Glycoproteins
- Neurons
- Receptors, Death Domain
- Spinal Cord Injuries