Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation.
Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation.
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DOI：
10.1371/journal.pone.0036542
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发表时间：
2012
期刊：
影响因子：
3.7
通讯作者：
Todi SV
中科院分区：
文献类型：
--
作者：
Blount JR;Burr AA;Denuc A;Marfany G;Todi SV
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately delivered to the proteasome for degradation. It is not well understood how ubiquitination of ERAD substrates is regulated. Here, we present evidence that the deubiquitinating enzyme Ubiquitin-Specific Protease 25 (USP25) is involved in ERAD. Our data support a model where USP25 counteracts ubiquitination of ERAD substrates by the ubiquitin ligase HRD1, rescuing them from degradation by the proteasome.
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影响因子：
16
作者：
Scaglione KM;Zavodszky E;Todi SV;Patury S;Xu P;Rodríguez-Lebrón E;Fischer S;Konen J;Djarmati A;Peng J;Gestwicki JE;Paulson HL
通讯作者：
Paulson HL
影响因子：
16
作者：
Meulmeester, Erik;Kunze, Marion;Melchior, Frauke
通讯作者：
Melchior, Frauke
影响因子：
3.3
作者：
Bernardi, Kaleena M.;Williams, Jeffrey M.;Tsai, Billy
通讯作者：
Tsai, Billy
影响因子：
16
作者：
Ernst, Robert;Mueller, Britta;Ploegh, Hidde L.;Schlieker, Christian
通讯作者：
Schlieker, Christian
影响因子：
46.9
作者：
Dantuma, NP;Lindsten, K;Masucci, MG
通讯作者：
Masucci, MG