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Mol. Cells 2007; 23(3): 391-397

Published online January 1, 1970

© The Korean Society for Molecular and Cellular Biology

Identification and Characterization of Two Novel Variants of the DUF1208 Protein FAM92A1

Xu Zhi Ruan, Fei Yan, Xin Yu Zhao, Chung Ting Wang, Ming Song, Han Suo Yang, Hong Xin Deng and Yu Quan Wei

Abstract

FAM92A1 (named FAM92A1-271) belongs to the family of proteins with conserved DUF1208 domains. Its function remains elusive. We identified two novel transcript variants (FAM92A1-251, FAM92A1-289) of FAM92A1. The presence of these transcripts in cancerous and normal cells, as well as their influence on cell prolifera-tion and apoptosis, were investigated. The subcellular location of FAM92A1 was determined by fluorescence microscopy. We found that FAM92A1-271 and FAM92A1- 289 were highly expressed in both normal and cancerous cells, but FAM92A1-251 was only expressed at a mo-derate level in both types of cell. Overexpression of FAM92A1-271, FAM92A1-251 and FAM92A1-289 in-hibited cell proliferation, caused S-phase arrest and induced apoptosis. Subcellular localization showed that FAM92A1 localizes to the nucleus. Our results show that FAM92A1 has different splicing variants, and that it may take part in regulating cell proliferation and apoptosis.

Keywords Alternative Splicing; Apoptosis; FAM92A1; RT-PCR; Subcellular Localization

Article

Research Article

Mol. Cells 2007; 23(3): 391-397

Published online June 30, 2007

Copyright © The Korean Society for Molecular and Cellular Biology.

Identification and Characterization of Two Novel Variants of the DUF1208 Protein FAM92A1

Xu Zhi Ruan, Fei Yan, Xin Yu Zhao, Chung Ting Wang, Ming Song, Han Suo Yang, Hong Xin Deng and Yu Quan Wei

Abstract

FAM92A1 (named FAM92A1-271) belongs to the family of proteins with conserved DUF1208 domains. Its function remains elusive. We identified two novel transcript variants (FAM92A1-251, FAM92A1-289) of FAM92A1. The presence of these transcripts in cancerous and normal cells, as well as their influence on cell prolifera-tion and apoptosis, were investigated. The subcellular location of FAM92A1 was determined by fluorescence microscopy. We found that FAM92A1-271 and FAM92A1- 289 were highly expressed in both normal and cancerous cells, but FAM92A1-251 was only expressed at a mo-derate level in both types of cell. Overexpression of FAM92A1-271, FAM92A1-251 and FAM92A1-289 in-hibited cell proliferation, caused S-phase arrest and induced apoptosis. Subcellular localization showed that FAM92A1 localizes to the nucleus. Our results show that FAM92A1 has different splicing variants, and that it may take part in regulating cell proliferation and apoptosis.

Keywords: Alternative Splicing, Apoptosis, FAM92A1, RT-PCR, Subcellular Localization

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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