Blots were incubated with antibodies that recognize X-IAP (Cell Signaling Technologies, Danvers, MA), RIP (BD Pharmigen), and FADD (BD Pharmigen ), and β-Actin (Sigma, St Louis, MO).
Cell suspensions containing each of the transiently transfected FLAG-IAP cells were combined with cells that transiently or stably expressed Smac56.
A family of proteins known as the inhibitors of apoptosis (IAPs) block cell death by interfering with the activity of key caspases.
In this report we investigated the impact of IAPs for cell death regulation in malignant melanoma.
This however is still a controversial issue and other studies show a suppressive effect of IAPs on cell mobility.
The first evidence for the role of IAPs in cell migration was demonstrated by Geisbrecht and Montell in 2004 during their studies with border cell migration in Drosophila ovaries, an important phenomenon for oogenesis during embryonic development.
Therefore, it necessitates a careful examination of coordinated Rac1-RhoA signaling pathways to predict the final migration phenotype in IAP-depleted cells.
To determine whether TNF-triggered death of MEFs with elevated RIPK3 used the same mechanism as when TNF caused death of IAP-depleted cells, we infected the caspase 8−/− and Ripk1−/− MEFs with the inducible lentiviral vector bearing FLAG-tagged RIPK3.
This observation prompted us to investigate the contribution of the IAP family in cell response to poly(I C) in a variety of human malignant cell types.
Survivin/BIRC5/API4/EPR-1 is an inhibitor of apoptosis protein (IAP) involved in cell survival, mitosis, stress response and developmental gene expression [ 50].
The role of IAP proteins in cell migration has been controversially discussed, as some studies reported that IAP proteins promote motility and migration, whereas others – similar to our findings – demonstrated that migration is enhanced on depletion of IAP proteins.
