Scientific background: |
RIPK1 (Regulator of G Protein Signaling 3), also called RIP, is an enzyme that in humans is encoded by the RIPK1 gene. Members of the TRAF protein family have been implicated in the activation of NF-kappa-B by the TNF superfamily. By yeast 2-hybrid and coimmunoprecipitation studies using mammalian cell extracts, Hsu et al. (1996) showed that RIP interacts with TRADD, TRAF1, TRAF2, and TRAF3. Hartz (2012) mapped the RIPK1 gene to chromosome 6p25.2 based on an alignment of the RIPK1 sequence with the genomic sequence. Stanger et al. (1995) found that overexpression of Rip in mammalian cells induced morphologic changes characteristic of apoptosis. They suggested that RIP may be an important element in the signal transduction machinery that mediates programmed cell death. |
References: |
1. Hartz, P. A. Personal Communication. Baltimore, Md. 10/26/2012.
2. Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., Goeddel, D. V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4: 387-396, 1996.
3. Stanger, B. Z., Leder, P., Lee, T.-H., Kim, E., Seed, B. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 81: 513-523, 1995.
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