Fig. 2: Domain structure and autoprocessing of PIDD1 protein, relative to reported mutations. | Translational Psychiatry

Fig. 2: Domain structure and autoprocessing of PIDD1 protein, relative to reported mutations.

From: Biallelic mutations in the death domain of PIDD1 impair caspase-2 activation and are associated with intellectual disability

Fig. 2

A Constitutive processing of PIDD gives rise to PIDD1-N (~48 kDa) and PIDD1-C (~51kDa). PIDD1-N contain a leucine-rich (LR) domain while PIDD1C contain a death domain between residues 774 to 893. S446 (generating PIDD1-C) and S588 (generating PIDD1-CC) are involved in this autoprocessing mechanism. PIDD1-C later undergoes further auto-cleavage resulting in the PIDD1-CC (~37 kDa) peptide. B Location of the mutations identified (p.R815W and p.Q863*) within the death domain of PIDD1 protein, and the prediction based on the exon-trap results for the effect of c.2275-1G>A, namely p.R759Gfs*1.

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