Full-length Fas-associated Death Domain Protein Interacts with Short Form of Cellular FLICE Inhibitory Protein 


Vol. 27,  No. 1, pp. 87-92, Jan.  2006
10.5012/bkcs.2006.27.1.087


PDF
  Abstract

Fas-associated death domain protein (FADD) recruits and activates procaspase-8 through interactions between the death effector domains of these two proteins. Cellular FLICE-inhibitory protein (c-FLIP) was identified as a molecule with sequence homology to caspase-8. It has been postulated that c-FLIP prevents formation of the competent death-inducing signaling complex in a ligand-dependent manner, through its interaction with FADD and/or caspase-8. However, the interaction of FADD and c-FLIS (short form) in apoptosis signaling has been controversially discussed. We show the purification and the characterization of human full-length FADD and c-FLIPS expressed in Escherichia coli. The purified FADD and c-FLIS are shown as homogeneity, respectively, in SDS-PAGE analysis and light-scattering measurements. The folding properties of the α-helical structure of FADD and the super-secondary structure of c-FLIS proteins were characterized by circular dichroism spectroscopy. Furthermore, we report here a series of biochemical and biophysical data for FADDc- FLIS binding in vitro. The binding of both FADD and c-FLIS proteins was detected by BIAcore biosensor, fluorescence measurement, and size-exclusion column (SEC).

  Statistics
Cumulative Counts from November, 2022
Multiple requests among the same browser session are counted as one view. If you mouse over a chart, the values of data points will be shown.


  Cite this article

[IEEE Style]

M. S. Jeong and S. B. Jang, "Full-length Fas-associated Death Domain Protein Interacts with Short Form of Cellular FLICE Inhibitory Protein," Bulletin of the Korean Chemical Society, vol. 27, no. 1, pp. 87-92, 2006. DOI: 10.5012/bkcs.2006.27.1.087.

[ACM Style]

Mi Suk Jeong and Se Bok Jang. 2006. Full-length Fas-associated Death Domain Protein Interacts with Short Form of Cellular FLICE Inhibitory Protein. Bulletin of the Korean Chemical Society, 27, 1, (2006), 87-92. DOI: 10.5012/bkcs.2006.27.1.087.

Search
(IN TITLE, AUTHOR, ABSTRACT,KEYWORDS)

Advanced Search ▼

POPULAR KEYWORDS
(TOP 10 KEYWORDS)

Recent Publications
(LAST 3 YEARS)

ISSN(Print) 0253-2964
ISSN(Online) 1229-5949