scholarly journals RING Finger Protein 38 Mediates LIM Domain Binding 1 Degradation and Regulates Cell Growth in Colorectal Cancer

2020 ◽  
Vol Volume 13 ◽  
pp. 371-379 ◽  
Author(s):  
Ziming Huang ◽  
Peng Yang ◽  
Hengfa Ge ◽  
Chenchen Yang ◽  
Yong Cai ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Cell Growth ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Lim Domain ◽  
Finger Protein

Ring Finger Protein 6 Exerts an Oncogenic Role in Colorectal Cancer by Activating WNT/β-Catenin Pathway Through TLE3 Ubiquitin Degradation

2017 ◽  
Vol 152 (5) ◽  
pp. S153
Author(s):  
Lei Liu ◽  
Yanquan Zhang ◽  
Jingwan Zhang ◽  
Yu Juan Dong ◽  
Francis K. Chan ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals The LIM domain protein UNC-95 is required for the assembly of muscle attachment structures and is regulated by the RING finger protein RNF-5 in C. elegans

2004 ◽  
Vol 165 (6) ◽  
pp. 857-867 ◽  
Author(s):  
Limor Broday ◽  
Irina Kolotuev ◽  
Christine Didier ◽  
Anindita Bhoumik ◽  
Benjamin Podbilewicz ◽  
...  
Keyword(s):  
Muscle Cell ◽  
Dense Body ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Lim Domain ◽  
Muscle Attachment ◽  
Dense Bodies ◽  
Finger Protein ◽  
Lim Domain Protein ◽  
Domain Protein

Here, we describe a new muscle LIM domain protein, UNC-95, and identify it as a novel target for the RING finger protein RNF-5 in the Caenorhabditis elegans body wall muscle. unc-95(su33) animals have disorganized muscle actin and myosin-containing filaments as a result of a failure to assemble normal muscle adhesion structures. UNC-95 is active downstream of PAT-3/β-integrin in the assembly pathways of the muscle dense body and M-line attachments, and upstream of DEB-1/vinculin in the dense body assembly pathway. The translational UNC-95::GFP fusion construct is expressed in dense bodies, M-lines, and muscle–muscle cell boundaries as well as in muscle cell bodies. UNC-95 is partially colocalized with RNF-5 in muscle dense bodies and its expression and localization are regulated by RNF-5. rnf-5(RNAi) or a RING domain deleted mutant, rnf-5(tm794), exhibit structural defects of the muscle attachment sites. Together, our data demonstrate that UNC-95 constitutes an essential component of muscle adhesion sites that is regulated by RNF-5.

miR-203a suppresses cell proliferation by targeting RING-finger protein 6 in colorectal cancer

2020 ◽  
Vol 31 (6) ◽  
pp. 583-591 ◽  
Author(s):  
Jiyu Miao ◽  
Ni Hou ◽  
Wanwan Yang ◽  
Qiuyu Jiang ◽  
Wanjuan Xue ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Cell Proliferation ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals miR-762 promotes porcine immature Sertoli cell growth via the ring finger protein 4 (RNF4) gene

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Changping Ma ◽  
Huibin Song ◽  
Lei Yu ◽  
Kaifeng Guan ◽  
Pandi Hu ◽  
...  
Keyword(s):  
Cell Growth ◽  
Sertoli Cell ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals Critical Role of the Ubiquitin Ligase Activity of UHRF1, a Nuclear RING Finger Protein, in Tumor Cell Growth

2005 ◽  
Vol 16 (12) ◽  
pp. 5621-5629 ◽  
Author(s):  
Yonchu Jenkins ◽  
Vadim Markovtsov ◽  
Wayne Lang ◽  
Poonam Sharma ◽  
Denise Pearsall ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Growth ◽  
Tumor Cell ◽  
A549 Cells ◽  
Ring Finger ◽  
Cell Cycle Checkpoints ◽  
Ring Finger Protein ◽  
E3 Ligases ◽  
Finger Protein ◽  
Nuclear Ring

Early cellular events associated with tumorigenesis often include loss of cell cycle checkpoints or alteration in growth signaling pathways. Identification of novel genes involved in cellular proliferation may lead to new classes of cancer therapeutics. By screening a tetracycline-inducible cDNA library in A549 cells for genes that interfere with proliferation, we have identified a fragment of UHRF1 (ubiquitin-like protein containing PHD and RING domains 1), a nuclear RING finger protein, that acts as a dominant negative effector of cell growth. Reduction of UHRF1 levels using an UHRF1-specific shRNA decreased growth rates in several tumor cell lines. In addition, treatment of A549 cells with agents that activated different cell cycle checkpoints resulted in down-regulation of UHRF1. The primary sequence of UHRF1 contains a PHD and a RING motif, both of which are structural hallmarks of ubiquitin E3 ligases. We have confirmed using an in vitro autoubiquitination assay that UHRF1 displays RING-dependent E3 ligase activity. Overexpression of a GFP-fused UHRF1 RING mutant that lacks ligase activity sensitizes cells to treatment with various chemotherapeutics. Taken together, our results suggest a general requirement for UHRF1 in tumor cell proliferation and implicate the RING domain of UHRF1 as a functional determinant of growth regulation.

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