scholarly journals Ubiquitin-specific protease 7 accelerates p14ARFdegradation by deubiquitinating thyroid hormone receptor-interacting protein 12 and promotes hepatocellular carcinoma progression

Hepatology ◽  
2015 ◽  
Vol 61 (5) ◽  
pp. 1603-1614 ◽  
Author(s):  
Jia-Bin Cai ◽  
Guo-Ming Shi ◽  
Zhao-Ru Dong ◽  
Ai-Wu Ke ◽  
Hong-Hui Ma ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Interacting Protein ◽  
Specific Protease ◽  
Ubiquitin Specific Protease

Evidence for evolutionary conservation of a physical linkage between the human BAF60b, a subunit of SWI/SNF complex, and thyroid hormone receptor interacting protein-1 genes on chromosome 17

Genome ◽  
1999 ◽  
Vol 42 (3) ◽  
pp. 545-549
Author(s):  
Rama Mohan Surabhi ◽  
Lisa Dawn Daly ◽  
Peter A Cattini
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Evolutionary Conservation ◽  
Chromosome 17 ◽  
N Gene ◽  
Interacting Protein ◽  
Physical Linkage ◽  
A Subunit ◽  
Polyadenylation Sites

The ubiquitously expressed rat BAF60b gene, which codes for a subunit of the multiprotein SWI/SNF complex, was recently identified between the pituitary growth hormone (GH-N) and thyroid hormone receptor interacting protein-1 (TRIP-1) genes. In primates, duplication of the GH-N gene has resulted in the addition of four placenta-specific (GH-V, CS-A, CS-B, and CS-L) genes downstream of the GH-N gene. As part of our study of the effect of remote sequences on the transcriptional regulation of the GH/CS gene family, we showed recently that these genes lie 40 kb upstream of the human TRIP-1 gene. We have now investigated the presence of the human BAF60b gene upstream of the TRIP-1 gene for evidence of evolutionary conservation of this arrangement or its disruption by the recent duplication of the nearby GH-N gene in primates. We report that, as in the rat genome, the human BAF60b gene is in the reverse transcriptional direction relative to the TRIP-1 gene, such that their polyadenylation sites are separated by 93 bp which compares with 92 bp in the rat. Reexamination of reported porcine TRIP-1 sequences also revealed the presence of the BAF60b gene separated by 93 bp, supporting an evolutionary conservation of this arrangement.Key words: P1 clone, gene mapping, downstream gene.

scholarly journals E3 Ubiquitin Ligase TRIP12: Regulation, Structure, and Physiopathological Functions

2020 ◽  
Vol 21 (22) ◽  
pp. 8515
Author(s):  
Manon Brunet ◽  
Claire Vargas ◽  
Dorian Larrieu ◽  
Jérôme Torrisani ◽  
Marlène Dufresne
Keyword(s):  
Thyroid Hormone ◽  
Ubiquitin Ligase ◽  
Hormone Receptor ◽  
Cell Cycle Progression ◽  
Thyroid Hormone Receptor ◽  
E3 Ubiquitin Ligase ◽  
Autism Spectrum ◽  
Causative Gene ◽  
Interacting Protein ◽  
C Terminus

The Thyroid hormone Receptor Interacting Protein 12 (TRIP12) protein belongs to the 28-member Homologous to the E6-AP C-Terminus (HECT) E3 ubiquitin ligase family. First described as an interactor of the thyroid hormone receptor, TRIP12’s biological importance was revealed by the embryonic lethality of a murine model bearing an inactivating mutation in the TRIP12 gene. Further studies showed the participation of TRIP12 in the regulation of major biological processes such as cell cycle progression, DNA damage repair, chromatin remodeling, and cell differentiation by an ubiquitination-mediated degradation of key protein substrates. Moreover, alterations of TRIP12 expression have been reported in cancers that can serve as predictive markers of therapeutic response. The TRIP12 gene is also referenced as a causative gene associated to intellectual disorders such as Clark–Baraitser syndrome and is clearly implicated in Autism Spectrum Disorder. The aim of the review is to provide an exhaustive and integrated overview of the different aspects of TRIP12 ranging from its regulation, molecular functions and physio-pathological implications.

scholarly journals Thyroid Hormone Receptor Interacting Protein 3 (Trip3) Is a Novel Coactivator of Hepatocyte Nuclear Factor-4 

Diabetes ◽  
2002 ◽  
Vol 51 (4) ◽  
pp. 910-914 ◽  
Author(s):  
H. Iwahashi ◽  
K. Yamagata ◽  
I. Yoshiuchi ◽  
J. Terasaki ◽  
Q. Yang ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Nuclear Factor ◽  
Hepatocyte Nuclear Factor ◽  
Interacting Protein ◽  
Hepatocyte Nuclear Factor 4
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