Cargando…
The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
The death inducing signaling complex (DISC) formed by the death receptor Fas, the adapter protein FADD and caspase-8 mediates the extrinsic apoptotic program. Mutations in Fas that disrupt the DISC cause autoimmune lymphoproliferative syndrome (ALPS). Here we show that the Fas–FADD death domain (DD)...
Autores principales: | Wang, Liwei, Yang, Jin Kuk, Kabaleeswaran, Venkataraman, Rice, Amanda J., Cruz, Anthony C., Park, Ah Young, Yin, Qian, Damko, Ermelinda, Jang, Se Bok, Raunser, Stefan, Robinson, Carol V., Siegel, Richard M., Walz, Thomas, Wu, Hao |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2988912/ https://www.ncbi.nlm.nih.gov/pubmed/20935634 http://dx.doi.org/10.1038/nsmb.1920 |
Ejemplares similares
-
The Fas/FADD death domain complex structure unravels signaling by receptor clustering
por: Scott, Fiona L., et al.
Publicado: (2008) -
Super-Resolution Imaging of Fas/CD95 Reorganization Induced by Membrane-Bound Fas Ligand Reveals Nanoscale Clustering Upstream of FADD Recruitment
por: Frazzette, Nicholas, et al.
Publicado: (2022) -
Fist/Hipk3: A FAS/Fadd-Interacting Serine/Threonine Kinase That Induces Fadd Phosphorylation and Inhibits FAS-Mediated Jun Nh(2)-Terminal Kinase Activation
por: Rochat-Steiner, Véronique, et al.
Publicado: (2000) -
Differential affinity of FLIP and procaspase 8 for FADD’s DED binding surfaces regulates DISC assembly
por: Majkut, J, et al.
Publicado: (2014) -
AFP promotes HCC progression by suppressing the HuR-mediated Fas/FADD apoptotic pathway
por: Chen, Tianke, et al.
Publicado: (2020)