2015
The melanoma-associated antigen 1 (MAGEA1) protein stimulates the E3 ubiquitin-ligase activity of TRIM31 within a TRIM31-MAGEA1-NSE4 complex
KOZÁKOVÁ, Lucie; Lucie VONDROVÁ; Karel STEJSKAL; Panagoula CHARALABOUS; Peter KOLESÁR et al.Základní údaje
Originální název
The melanoma-associated antigen 1 (MAGEA1) protein stimulates the E3 ubiquitin-ligase activity of TRIM31 within a TRIM31-MAGEA1-NSE4 complex
Název česky
Protein melanoma-associated antigen 1 (MAGEA1) stimuluje E3 ubikvitin-ligasovou aktivitu TRIM31 v rámci komplexu TRIM31-MAGEA1-NSE4
Autoři
KOZÁKOVÁ, Lucie ORCID; Lucie VONDROVÁ; Karel STEJSKAL; Panagoula CHARALABOUS; Peter KOLESÁR; Alan R. LEHMANN; Stjepan ULDRIJAN; Christopher M. SANDERSON; Zbyněk ZDRÁHAL a Jan PALEČEK
Vydání
Cell Cycle, Philadelphia, Taylor&Francis Inc, 2015, 1538-4101
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10601 Cell biology
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 3.952
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14740/15:00080494
Organizační jednotka
Středoevropský technologický institut
UT WoS
EID Scopus
Klíčová slova česky
E3 ubikvitin ligasa; MAGEA1; melanoma-associated antigen; MDM4; NSE1-NSE3-NSE4 komplex; NSE4; EID proteinová rodina; evoluce proteinů; PCGF6; RING-finger proteiny; RNF166; TRIM31; TRAF6; TRIM8; TRIM41; ubikvitinace
Klíčová slova anglicky
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
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 13. 3. 2018 15:37, Mgr. Lucie Jarošová, DiS.
Anotace
V originále
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.
Návaznosti
| ED1.1.00/02.0068, projekt VaV |
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| EE2.3.20.0189, projekt VaV |
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| EE2.3.30.0037, projekt VaV |
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| GA13-00774S, projekt VaV |
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| GA14-12166S, projekt VaV |
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| GBP206/12/G151, projekt VaV |
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| IAA501630902, projekt VaV |
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