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@article{1298092,
author = {Kozáková, Lucie and Vondrová, Lucie and Stejskal, Karel and Charalabous, Panagoula and Kolesár, Peter and Lehmann, Alan R. and Uldrijan, Stjepan and Sanderson, Christopher M. and Zdráhal, Zbyněk and Paleček, Jan},
article_location = {Philadelphia},
article_number = {6},
doi = {http://dx.doi.org/10.1080/15384101.2014.1000112},
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},
language = {eng},
issn = {1538-4101},
journal = {Cell Cycle},
title = {The melanoma-associated antigen 1 (MAGEA1) protein stimulates the E3 ubiquitin-ligase activity of TRIM31 within a TRIM31-MAGEA1-NSE4 complex},
url = {http://www.tandfonline.com/doi/pdf/10.1080/15384101.2014.1000112},
volume = {14},
year = {2015}
}
TY - JOUR
ID - 1298092
AU - Kozáková, Lucie - Vondrová, Lucie - Stejskal, Karel - Charalabous, Panagoula - Kolesár, Peter - Lehmann, Alan R. - Uldrijan, Stjepan - Sanderson, Christopher M. - Zdráhal, Zbyněk - Paleček, Jan
PY - 2015
TI - The melanoma-associated antigen 1 (MAGEA1) protein stimulates the E3 ubiquitin-ligase activity of TRIM31 within a TRIM31-MAGEA1-NSE4 complex
JF - Cell Cycle
VL - 14
IS - 6
SP - 920-930
EP - 920-930
PB - Taylor&Francis Inc
SN - 15384101
KW - E3 ubiquitin ligase
KW - MAGEA1
KW - melanoma-associated antigen family
KW - MDM4
KW - NSE1-NSE3-NSE4 complex
KW - NSE4
KW - EID family
KW - protein evolution
KW - PCGF6
KW - RING-finger proteins
KW - RNF166
KW - TRIM31
KW - TRIM family
KW - TRAF6
KW - TRIM8
KW - TRIM41
KW - ubiquitination
UR - http://www.tandfonline.com/doi/pdf/10.1080/15384101.2014.1000112
L2 - http://www.tandfonline.com/doi/pdf/10.1080/15384101.2014.1000112
N2 - 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.
ER -
KOZÁKOVÁ, Lucie, Lucie VONDROVÁ, Karel STEJSKAL, Panagoula CHARALABOUS, Peter KOLESÁR, Alan R. LEHMANN, Stjepan ULDRIJAN, Christopher M. SANDERSON, Zbyněk ZDRÁHAL a Jan PALEČEK. The melanoma-associated antigen 1 (MAGEA1) protein stimulates the E3 ubiquitin-ligase activity of TRIM31 within a TRIM31-MAGEA1-NSE4 complex. \textit{Cell Cycle}. Philadelphia: Taylor\&{}Francis Inc, 2015, roč.~14, č.~6, s.~920-930. ISSN~1538-4101. Dostupné z: https://dx.doi.org/10.1080/15384101.2014.1000112.
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