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Posttranscriptional control of intestinal epithelium homeostasis by RNA-binding protein HuR

LIU Xiangzheng^1,2, XIAO Lan^1,2, WANG Jian-Ying^1,2,3,*

¹Cell Biology Group, Department of Surgery, University of Maryland School of Medicine, Baltimore, MD 21201, USA ；²Baltimore Veterans Affairs Medical Center, Baltimore, MD 21201, USA；³Department of Pathology, University of Maryland School of Medicine, Baltimore, MD 21201, USA

Abstract

The mammalian intestinal epithelium is a rapidly self-renewing tissue in the body and directly interfaces with a wide array of luminal noxious contents and microorganisms. Homeostasis of the intestinal epithelium is preserved through well-controlled mechanisms including posttranscriptional regulation. RNA-binding protein (RBP) HuR regulates the stability and translation of target mRNAs and is intimately involved in many aspects of gut mucosal pathophysiology. Here we highlight the biological roles of HuR in maintaining the integrity of the intestinal epithelium, with particular focus on the emerging evidence of HuR in the regulation of intestinal epithelial renewal, mucosal repair, defense, and gut permeability. We also further analyze the mechanisms through which HuR and its interactions with other RBPs and noncoding RNAs (ncRNAs) such as microRNAs and long ncRNAs modulate the intestinal epithelial homeostasis. With rapidly advancing knowledge of RBPs and ncRNAs, there is growing recognition that posttranscriptional control of the intestinal epithelium homeostasis might be promising therapeutic targets in our efforts to protect the integrity of the intestinal epithelium under critical pathological conditions.

Key words: RNA-binding proteins; noncoding RNAs; intestinal epithelial renewal; mucosal repair; gut permeability

Received: 2019-10-28　　Accepted: 2020-02-13

Corresponding author: 汪建英　　E-mail: jywang@som.umaryland.edu

DOI: 10.13294/j.aps.2020.0034

Citing This Article：

LIU Xiangzheng, XIAO Lan, WANG Jian-Ying. Posttranscriptional control of intestinal epithelium homeostasis by RNA-binding protein HuR. Acta Physiol Sin 2020; 72 (3): 325-335