Schematic depiction of proteins involved in the division of POs and mitochondria in yeast and mammals. Domains with specific functions/characteristics are shown and retained in the other figures. VD, variable domain; TPR, tetratricopeptide repeat; TMD, transmembrane domain; AH1–H4, putative amphipathic helices based on the work on P. pastoris Pex11 (Zientara-Rytter et al., 2022); *Conserved, N-terminal AH in Pex11, termed Pex11-Amph, necessary for peroxisomal fission in vivo and for tubulation of liposomes with a lipid consistency resembling the peroxisomal membrane (Opaliński et al., 2011); CC, coiled-coil; NBD, nucleotide-binding domain. No protein domains have been reported for Pex27. Protein lengths indicate the number of amino acids (aa) in yeast (S. cerevisiae) or mammalian (human) proteins. DNM2 (870 aa) is not shown but it has domains similar to DRP1. All figures were prepared using Biorender.com.