A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its ‘death domain’
- 19 June 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 367 (1), 39-44
- https://doi.org/10.1016/0014-5793(95)00534-g
Abstract
A novel protein that binds specifically to the intracellular domain of the p55 tumor necrosis factor (TNF) receptor was cloned by two-hybrid screening of a HeLa cell cDNA library. Data bank searches revealed high sequence similarity of the protein (55.11) to yeast, nematode and plant proteins, whose functions are yet unknown. Significant similarity was also found between 55.11 and SEN3, the yeast equivalent of the p112 subunit of the 26S proteasome. Deletion analysis showed that the protein binds to the p55 receptor upstream to the region involved in induction of cell deathThis publication has 14 references indexed in Scilit:
- A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death DomainOnline Journal of Public Health Informatics, 1995
- Self-association of the “Death Domains” of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 EffectsOnline Journal of Public Health Informatics, 1995
- Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signalingCell, 1994
- A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptorCell, 1994
- KEKE motifsFEBS Letters, 1994
- A novel domain within the 55 kd TNF receptor signals cell deathCell, 1993
- Solubilization and Purification of Enzymatically Active Glutathione S-Transferase (pGEX) Fusion ProteinsAnalytical Biochemistry, 1993
- Tumor necrosis factor.Online Journal of Public Health Informatics, 1991
- A novel genetic system to detect protein–protein interactionsNature, 1989
- TUMOR NECROSIS, CACHEXIA, SHOCK, AND INFLAMMATION: A COMMON MEDIATORAnnual Review of Biochemistry, 1988