scholarly journals Deubiquitinase ubiquitin‐specific protease 9X regulates the stability and function of E3 ubiquitin ligase ring finger protein 115 in breast cancer cells

2019 ◽  
Vol 110 (4) ◽  
pp. 1268-1278 ◽  
Author(s):  
Qin Lu ◽  
Dayun Lu ◽  
Zhi‐Ming Shao ◽  
Da‐Qiang Li
Keyword(s):  
Ubiquitin Ligase ◽  
Breast Cancer Cells ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
The Stability ◽  
And Function

scholarly journals Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4)

2015 ◽  
Vol 290 (25) ◽  
pp. 15526-15537 ◽  
Author(s):  
Ivo A. Hendriks ◽  
Joost Schimmel ◽  
Karolin Eifler ◽  
Jesper V. Olsen ◽  
Alfred C. O. Vertegaal
Keyword(s):  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein ◽  
Specific Protease ◽  
Ubiquitin Specific Protease

scholarly journals Ring Finger Protein 149 Is an E3 Ubiquitin Ligase Active on Wild-type v-Raf Murine Sarcoma Viral Oncogene Homolog B1 (BRAF)

2012 ◽  
Vol 287 (28) ◽  
pp. 24017-24025 ◽  
Author(s):  
Seung-Woo Hong ◽  
Dong-Hoon Jin ◽  
Jae-Sik Shin ◽  
Jai-Hee Moon ◽  
Young-Soon Na ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Wild Type ◽  
Viral Oncogene ◽  
Finger Protein ◽  
Type V ◽  
Murine Sarcoma ◽  
Viral Oncogene Homolog

scholarly journals Human RING finger protein ZNF645 is a novel testis-specific E3 ubiquitin ligase

2010 ◽  
Vol 12 (5) ◽  
pp. 658-666 ◽  
Author(s):  
Yun-Qiang Liu ◽  
Gang Bai ◽  
Hao Zhang ◽  
Dan Su ◽  
Da-Chang Tao ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals The vertebrate muscle-specific RING finger protein family includes MuRF4 - A novel, conserved E3-ubiquitin ligase

FEBS Letters ◽  
2014 ◽  
Vol 588 (23) ◽  
pp. 4390-4397 ◽  
Author(s):  
Daniel J. Macqueen ◽  
Eduardo N. Fuentes ◽  
Juan Antonio Valdés ◽  
Alfredo Molina ◽  
Samuel A.M. Martin
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Protein Family ◽  
Ring Finger Protein ◽  
Finger Protein ◽  
Vertebrate Muscle

Mouse RING finger protein Rnf133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase

Cell Research ◽  
2008 ◽  
Vol 18 (7) ◽  
pp. 800-802 ◽  
Author(s):  
Hong Nian ◽  
Wei Zhang ◽  
Hexin Shi ◽  
Qingzhen Zhao ◽  
Qi Xie ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals Porcine RING Finger Protein 114 Inhibits Classical Swine Fever Virus Replication via K27-Linked Polyubiquitination of Viral NS4B

2019 ◽  
Vol 93 (21) ◽  
Author(s):  
Yuexiu Zhang ◽  
Huawei Zhang ◽  
Guang-Lai Zheng ◽  
Qian Yang ◽  
Shaoxiong Yu ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Classical Swine Fever ◽  
Ring Domain ◽  
Ring Finger Protein ◽  
E3 Ligases ◽  
Finger Protein ◽  
Ubiquitin Ligase Activity ◽  
Ns4b Protein

ABSTRACT In the host, many RING domain E3 ligases have been reported to inhibit viral replication through various mechanisms. In a previous screen, we found that porcine RING finger protein 114 (pRNF114), a RING domain E3 ubiquitin ligase, inhibits classical swine fever virus (CSFV) replication. This study aimed to clarify the underlying antiviral mechanism of pRNF114 against CSFV. Upon CSFV infection, pRNF114 mRNA was upregulated both in vitro and in vivo. CSFV replication was significantly suppressed in PK-pRNF114 cells stably expressing pRNF114 by the lentivirus-delivered system, whereas CSFV growth was enhanced in PK-15 cells with RNF114 knockout by the CRISPR/Cas9 system. The RING domain of pRNF114, which has E3 ubiquitin ligase activity, is crucial for its antiviral activity. Mechanistically, pRNF114 interacted with the CSFV NS4B protein through their C-terminal domains, which led to the K27-linked polyubiquitination and degradation of NS4B through a proteasome-dependent pathway. Collectively, these findings indicate that pRNF114 as a critical regulator of CSFV replication and uncover a mechanism by which pRNF114 employs its E3 ubiquitin ligase activity to inhibit CSFV replication. IMPORTANCE Porcine RING finger protein 114 (pRNF114) is a member of the RING domain E3 ligases. In this study, it was shown that pRNF114 is a potential anti-CSFV factor and the anti-CSFV effect of pRNF114 depends on its E3 ligase activity. Notably, pRNF114 targets and catalyzes the K27-linked polyubiquitination of the NS4B protein and then promotes proteasome-dependent degradation of NS4B, inhibiting the replication of CSFV. To our knowledge, pRNF114 is the first E3 ligase to be identified as being involved in anti-CSFV activity, and targeting NS4B could be a crucial route for antiviral development.

Ubiquitin-specific protease 19 regulates the stability of the E3 ubiquitin ligase MARCH6

2014 ◽  
Vol 328 (1) ◽  
pp. 207-216 ◽  
Author(s):  
Nobuhiro Nakamura ◽  
Kumi Harada ◽  
Masako Kato ◽  
Shigehisa Hirose
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
The Stability
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