E3 Ubiquitin Ligase TRIP12: Regulation, Structure, and Physiopathological Functions.

International Journal of Molecular Sciences
M BrunetMarlène Dufresne

Abstract

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.

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Citations

Feb 13, 2021·Journal of Gastroenterology and Hepatology·Yue WuJianping Gong

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Methods Mentioned

BETA
ubiquitination
neddylation
exome sequencing
RNA-seq
transgenic

Software Mentioned

BLASTP
Gepia2 Gene Expression Profiling Interactive Analysis
COBALT ( Constraint - based Multiple Alignment Tool )
PHI
PhosphoSitePlus
IDEAL
cBioPortal
InterProScan
COBALT
EMBOSS Matcher

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