Publication details

The melanoma-associated antigen 1 (MAGEA1) protein stimulates the E3 ubiquitin-ligase activity of TRIM31 within a TRIM31-MAGEA1-NSE4 complex

Authors

KOZÁKOVÁ Lucie VONDROVÁ Lucie STEJSKAL Karel CHARALABOUS Panagoula KOLESÁR Peter LEHMANN Alan R. ULDRIJAN Stjepan SANDERSON Christopher M. ZDRÁHAL Zbyněk PALEČEK Jan

Year of publication 2015
Type Article in Periodical
Magazine / Source Cell Cycle
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.tandfonline.com/doi/pdf/10.1080/15384101.2014.1000112
Doi http://dx.doi.org/10.1080/15384101.2014.1000112
Field Genetics and molecular biology
Keywords E3 ubiquitin ligase; MAGEA1; melanoma-associated antigen family; MDM4; NSE1-NSE3-NSE4 complex; NSE4; EID family; protein evolution; PCGF6; RING-finger proteins; RNF166; TRIM31; TRIM family; TRAF6; TRIM8; TRIM41; ubiquitination
Attached files
Description The MAGE (Melanoma-associated antigen) protein family members are structurally related to each other by a MAGE-homology domain comprised of 2 winged helix motifs WH/A and WH/B. This family specifically evolved in placental mammals although single homologs designated NSE3 (non-SMC element) exist in most eukaryotes. NSE3, together with its partner proteins NSE1 and NSE4 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex. Previously, we showed that interactions of the WH/B motif of the MAGE proteins with their NSE4/EID partners are evolutionarily conserved (including the MAGEA1-NSE4 interaction). In contrast, the interaction of the WH/A motif of NSE3 with NSE1 diverged in the MAGE paralogs. We hypothesized that the MAGE paralogs acquired new RING-finger-containing partners through their evolution and form MAGE complexes reminiscent of NSE1-NSE3-NSE4 trimers. In this work, we employed the yeast 2-hybrid system to screen a human RING-finger protein library against several MAGE baits. We identified a number of potential MAGE-RING interactions and confirmed several of them (MDM4, PCGF6, RNF166, TRAF6, TRIM8, TRIM31, TRIM41) in co-immunoprecipitation experiments. Among these MAGE-RING pairs, we chose to examine MAGEA1-TRIM31 in detail and showed that both WH/A and WH/B motifs of MAGEA1 bind to the coiled-coil domain of TRIM31 and that MAGEA1 interaction stimulates TRIM31 ubiquitin-ligase activity. In addition, TRIM31 directly binds to NSE4, suggesting the existence of a TRIM31-MAGEA1-NSE4 complex reminiscent of the NSE1-NSE3-NSE4 trimer. These results suggest that MAGEA1 functions as a co-factor of TRIM31 ubiquitin-ligase and that the TRIM31-MAGEA1-NSE4 complex may have evolved from an ancestral NSE1-NSE3-NSE4 complex.
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