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Sachie Nakamichi, Yoko Senga, Hiroshi Inoue, Aki Emi, Yasushi Matsuki, Eijiro Watanabe, Ryuji Hiramatsu, Wataru Ogawa, and Masato Kasuga

Rnf128 ) is a transmembrane RING finger-type E3 ubiquitin ligase. The abundance of GRAIL mRNA is increased in T-lymphocytes in response to the induction of anergy ( Anandasabapathy et al . 2003 ), and the encoded protein plays an important role in the

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Kristine M Wadosky, Jessica M Berthiaume, Wei Tang, Makhosi Zungu, Michael A Portman, A Martin Gerdes, and Monte S Willis

( Kopf et al. 2000 ). The muscle-specific ubiquitin ligase MuRF1 has recently been shown to specifically inhibit PPARα, but not PPARβ/ or PPARγ1, activity in vivo ( Rodriguez et al. 2015). In contrast to the previous studies on nuclear receptors

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Wei-Ling Fang, Si-Yi Lai, Wei-An Lai, Ming-Ting Lee, Ching-Fong Liao, Ferng-Chun Ke, and Jiuan-Jiuan Hwang

that a Cx43-interacting protein, ubiquitin-ligase Nedd4, is involved in the regulation of internalization and degradation of Cx43 gap junction ( Leykauf et al . 2006 , Mollerup et al . 2011 ). Accordingly, we were interested to understand the role of

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Nina Gustafsson Sheppard, Nina Heldring, and Karin Dahlman-Wright

stimulation has been reported ( Ellison-Zelski et al . 2009 ). However, in breast cancer, this inverse relationship between ERα and its agonist is lost, indicating deregulation of ERα expression ( Khan et al . 1999 ). RBCK1 is an E3 ubiquitin ligase

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Jiayu Zhang, Chengwei Chen, Liang Wu, Qiang Wang, Jiawei Chen, Sifang Zhang, and Zhenguo Chen

H 2018 The NRF2-PGC-1β pathway activates kynurenine aminotransferase 4 via attenuation of an E3 ubiquitin ligase, synoviolin, in a cecal ligation/perforation-induced septic mouse model . Molecular Medicine Reports 18 2467 – 2475 . ( https

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Xu-guang Zhu, Dong Wook Kim, Michael L Goodson, Martin L Privalsky, and Sheue-Yann Cheng

adipogenesis was accompanied by progressive loss of NCoR1 protein. The downregulation of NCoR1 depended on the TRs and the ubiquitin ligase mSiah2. A more severe impairment of T 3 -stimulated adipogenesis in L1-α1PV cells than in L1-β1PV cells was associated

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LK Beitel, YA Elhaji, R Lumbroso, SS Wing, V Panet-Raymond, B Gottlieb, L Pinsky, and MA Trifiro

The androgen receptor (AR) N-terminal domain plays a critical role in androgen-responsive gene regulation. A novel AR N-terminal-interacting protein (ARNIP) was isolated using the yeast two-hybrid system and its interaction with amino acids 11-172 of the normal or corresponding region of the polyglutamine-expanded human AR confirmed by glutathione S-transferase pulldown assays. ARNIP cDNAs cloned from NSC-34 (mouse neuroblastoma/spinal cord) or PC-3 (human prostate adenocarcinoma) mRNA encoded highly homologous 30 kDa (261 amino acids) cysteine-rich proteins with a RING-H2 (C3H2C3 zinc finger) domain; this motif is highly conserved in predicted ARNIP-homologous proteins from several other species. Expression of the approximately 1.7 kb ARNIP mRNA was detected in various tissues by Northern blotting, but was highest in mouse testes, kidney and several neuronal cell lines. In addition, the human ARNIP protein was found to be encoded by nine exons spanning 32 kb on chromosome 4q21. In COS-1 cells, coexpression of ARNIP and AR did not affect AR ligand-binding kinetics, nor did ARNIP act as a coactivator or corepressor in transactivation assays. However, AR N-terminal:C-terminal interaction was reduced in the presence of ARNIP. Intriguingly, ARNIP, and in particular its RING-H2 domain, functioned as a ubiquitin-protein ligase in vitro in the presence of a specific ubiquitin-conjugating enzyme, Ubc4-1. Mutation of a single cysteine residue in the ARNIP RING-H2 domain (Cys145Ala) abolished this E3 ubiquitin ligase activity. Fluorescent protein tagging studies revealed that AR-ARNIP interaction was hormone-independent in COS-1 cells, and suggest that colocalization of both AR and ARNIP to the nucleus upon androgen addition may allow ARNIP to play a role in nuclear processes. Thus, identification of a novel AR-interacting protein with ubiquitin ligase activity will stimulate further investigation into the role of ubiquitination and the ubiquitin-proteasome system in AR-mediated cellular functions.

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H K Kinyamu, J Chen, and T K Archer

a lysine residue in the target protein bound to a specific E3 ubiquitin ligase (Fig. 1 ). Depending on the type of E3 ligase, the transfer of ubiquitin to the substrate is either direct or indirect. In most organisms, including humans and yeast, a

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Kyle T Helzer, Christopher Hooper, Shigeki Miyamoto, and Elaine T Alarid

conserved catalytic cysteine residue of the E2 enzyme, forming a thioester-linked E2-Ub complex in a process known as transthioesterification ( Lee & Schindelin 2008 ). Lastly, the third class of enzymes, known as E3 ubiquitin ligases, facilitates the

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Péter Egri and Balázs Gereben

defined. We aimed to determine the combination of molecular features required and sufficient to allow an activating deiodinase to be targeted by E3 ubiquitin ligases, a pre-requisite for proteins processed along the ubiquitin–proteasome pathway. We