Skip to main content
. 2022 Nov 21;23(12):e55420. doi: 10.15252/embr.202255420

Figure 2. Genetic, physical, and functional interaction network of transition zone proteins.

Figure 2

Interactions within the ring include among the most evolutionarily conserved transition zone (TZ) proteins, and interactions with other selected TZ proteins are shown outside of the ring in gray dotted boxes. Genetic interactions between two genes encoding TZ proteins (circles) and/or TZ protein localization dependency (arrows point to dependent protein) are shown on gray connecting lines and colored according to the model organism (Chlamydomonas, purple; Drosophila, blue, C. elegans, green, and vertebrates, red). Direct physical interactions and co‐precipitation of proteins are represented by yellow dotted and solid connections, respectively (wine‐colored dotted lines depict both types of interactions). Tentative grouping of proteins into MKS, NPHP or core scaffolding modules are colored purple, blue and green, respectively; uncertain grouping is shown as gray. Proteins are shown alongside their ciliopathy associations (MKS, Meckel syndrome; JBTS, Joubert syndrome; BBS, Bardet–Biedl syndrome; NPHP, Nephronophthisis; OFD, Orofaciodigital syndrome; COACH, COACH syndrome; SLSN, Senior–Løken syndrome; LCA, Leber congenital amaurosis) as well as domain structures (C2 and related B9 domains; TM, transmembrane; CC, coiled coil; β‐prop, β‐propeller; SH3, SRC homology 3; CYS, cysteine‐rich; MSP, major sperm protein). See text for additional details. All interaction data are presented in Table EV1.