This entry includes death effector domain-containing proteins, DEDD and DEDD2. DEDD is a scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis []. DEDD2 is involved in the regulation of nuclear events mediated by the extrinsic apoptosis pathway [].
Gasdermin-E, also known as DFNA5, is involved in the p53-regulated cellular response to response to DNA damage probably by cooperating with p53 []. It can be cleaved by CASP3 into two parts: GSDME-N and GSDME-C. The GSDME-N fragment can perforate membranes and thereby induce pyroptosis []. Purified GSDME-N has been shown to efficiently lyse phosphoinositide/cardiolipin-containing liposomes and form pores on membranes made of artificial or natural phospholipid mixtures [].
Proteins in this family contain a CPL domain, which is a C-terminal domain found in Penguin-like proteins, and Pumilio RNA-binding repeats. Proteins include the following:Pumilio homologue 3 (PUM3; also known as Puf-A), which inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress []. Tertiary structure determination has revealed that PUM3 has eleven PUM repeats arranged in an L-shape, and in contrast to classical PUF proteins, PUM3 forms sequence-independent interactions with DNA or RNA, mediated by conserved basic residues [].Pumilio homology domain family member 6 from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which is an RNA-binding protein involved in post-transcriptional regulation and represses ASH1 mRNA translation. ASH1 is a a protein determinant for mating-type switching [].Protein penguin from Drosophila melanogaster.
