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. 2018 Dec 10;294(6):1944–1955. doi: 10.1074/jbc.RA118.004928

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© 2019 Dionne et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 8. — Protein complexes revolving around extraribosomal uS5. Shown is a schematic of independent PDCD2–uS5–PRMT3 (upper left) and PDCD2L–uS5-PRMT3 (upper right) complexes as we have described in humans (29). Mutually exclusive interactions of uS5 with ZNF277 and PRMT3 result in the formation of PDCD2–uS5–ZNF277 (lower left) and PDCD2L–uS5–ZNF277 (lower right) complexes. The existence of conserved complexes in Drosophila is supported by results from high-throughput two-hybrid screening and biochemical studies (28, 30), showing that homologs of PRMT3 (Art3), ZNF277 (CG9890), PDCD2 (Zfrp8), and PDCD2L (Trus) interact with uS5 (Sop).