Fig. 1: Pedigree and PIEZO1 compound heterozygous mutations in a PBS patient. | Nature Communications

Fig. 1: Pedigree and PIEZO1 compound heterozygous mutations in a PBS patient.

From: PIEZO1 loss-of-function compound heterozygous mutations in the rare congenital human disorder Prune Belly Syndrome

Fig. 1

a Pedigree of the proband family showing the origin of his compound heterozygous PIEZO1 variants. The affected male (II.2) is indicated with an arrow and a black square. The carrier father (I.1) and the carrier mother (I.2) are shown by a central black line. Individuals without available DNA are outlined in red (II.1 and II.3). Males = square, female = circle, miscarriage unknown sex = triangle. b Cryo-EM trimeric mPiezo1 structure (Protein Data Bank ID #6B3R). mPiezo1 blades (gray) encompass residues 577–2123. Pore domain (green) spans from 2124 to 2547 residues. Human PBS pore domain variant at S2195L (murine S2211L) is shown as red spheres on all three monomers. Since amino acids 1-576 are not structurally resolved, the human PBS variant G253R (murine S260R) is not shown but is predicted to be within the lipid bilayer. c Schematic representation of the missense PIEZO1 variants in PBS male in the region encoding the protein domains. d Multiple sequence alignment on PIEZO1 mutated residues, showing that the G253 residue is not conserved in mouse, rat, cow, and zebrafish. However, the S2195 mutated residue is highly conserved among vertebrate species analyzed, suggesting that this residue plays an important role in PIEZO1 function.

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