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Distinct assemblies and interactomes of the nuclear and cytoplasmic mammalian CTLH E3 ligase complex.

The C-terminal to LisH (CTLH) complex is a newly discovered multi-subunit E3 ubiquitin ligase whose cellular functions are poorly characterized. While some CTLH subunits have been found to localize in both the nucleus and cytoplasm of mammalian cells, differences between the compartment-specific complexes have not been explored. Here, we show that the CTLH complex forms different molecular weight complexes in nuclear and cytoplasmic fractions. Loss of WDR26 severely decreases nuclear CTLH complex subunit levels and impairs higher-order CTLH complex formation, revealing WDR26 as a critical determinant of CTLH complex nuclear stability. Through affinity purification coupled to mass spectrometry (AP-MS) of endogenous CTLH complex member RanBPM from nuclear and cytoplasmic fractions, we identified over 170 compartment-specific interactors involved in various conserved biological processes such as ribonucleoprotein biogenesis and chromatin assembly. We validated the nuclear-specific RanBPM interaction with macroH2A1 and the cytoplasmic-specific interaction with Tankyrase-1/2. Overall, this study provides critical insights into CTLH complex function and composition in both the cytoplasm and nucleus.