The LCB2 subunit of the sphingolip biosynthesis enzyme serine palmitoyltransferase can function as an attenuator of the hypersensitive response and Bax-induced cell death. 
Previous results showed that expression of the gene encoding the LONG-CHAIN BASE2 (LCB(2)) subunit of serine palmitoyltransferase (SPT), designated BcLCB(2), from nonheading Chinese cabbage (Brassica campestris ssp.  chinensis) was up-regulated during hypersensitive cell death (HCD) induced by the Phytophthora boehmeriae elicitor PB90.  Overexpression of BcLCB(2) in Nicotiana tabacum leaves suppressed the HCD normally initiated by elicitors and PB90-triggered H(2)O(2) accumulation.  BcLCB(2) also functioned as a suppressor of mouse Bcl-2 associated X (Bax) protein-mediated HCD and cell death caused by Ralstonia solanacearum.  BcLCB(2) overexpression suppressed Bax- and oxidant stress-triggered yeast cell death.  Reactive oxygen species (ROS) accumulation induced by Bax was compromised in BcLCB(2)-overexpressing yeast cells.  The findings that NbLCB(2) silencing in Nicotiana benthamiana enhanced elicitor-triggered HCD, combined with the fact that myriocin, a potent inhibitor of SPT, had no effect on Bax-induced programmed cell death, suggested that suppression of cell death was not involved in the dominant-negative effect that resulted from BcLCB(2) overexpression.  A BcLCB(2) mutant assay showed that the suppression was not involved in SPT activity.  The results suggest that plant HCD and stress-induced yeast cell death might share a common signal transduction pathway involving LCB(2), and that LCB(2) protects against cell death by inhibiting ROS accumulation, this inhibition being independent of SPT activity.