ARMET is a Soluble ER Protein Induced by the Unfolded Protein Response via ERSE-II Element

Cell Structure and Function

Jun-ichi Nozaki²  Kazuhiro Nagata²  Hiroshi Kubota²  Motoko Naitoh²  Naomi Mizobuchi²  Akio Koizumi¹  Jun Hoseki²  Shinya Toyokuni³ 

[1] Department of Health and Environmental Sciences, Graduate School of Medicine and Faculty of Medicine, Kyoto University;Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University;Department of Pathology and Biology of Diseases, Kyoto University Graduate School of Medicine

关键词: endoplasmic reticulum;    unfolded protein response;    transcriptional regulation;    cis-acting element;    disulfide bond;   

DOI  :  10.1247/csf.07001

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(28)Cited-By(37)Arginine rich, mutated in early stage of tumors (ARMET) was first identified as a human gene highly mutated in a variety of cancers. However, little is known about the characteristics of the ARMET protein and its expression. We identified ARMET as a gene upregulated by endoplasmic reticulum (ER) stress. Here, we show that the mouse homologue of ARMET is an 18-kDa soluble ER protein that is mature after cleavage of a signal sequence and has four intramolecular disulfide bonds, including two in CXXC sequences. ER stress stimulated ARMET expression, and the expression patterns of ARMET mRNA and protein in mouse tissues were similar to those of Grp78, an Hsp70-family protein required for quality control of proteins in the ER. A reporter gene assay using a mouse ARMET promoter revealed that the unfolded protein response of the ARMET gene is regulated by an ERSE-II element whose sequence is identical to that of the HERP gene. ARMET is the second fully characterized ERSE-II-dependent gene and likely contributes to quality control of proteins in the ER.

【 授权许可】

Unknown