Related Experiment Video
Updated: May 12, 2026

Pharmacologic Induction of Epidermal Melanin and Protection Against Sunburn in a Humanized Mouse Model
Published on: September 7, 2013
Protective role of the endoplasmic reticulum protein mitsugumin23 against ultraviolet C-induced cell death
Arisa Yamashita1, Tatsuya Taniwaki, Yuka Kaikoi
1Department of Molecular Cell Biology and Medicine, Institute of Health Biosciences, The University of Tokushima Graduate School, Tokushima 770-8505, Japan.
Abstract:
The endoplasmic reticulum (ER) operates in adaptive responses to various stresses, dictating cell fate. Here we show that knockdown of the ER protein mitsugumin23 (MG23) enhances cell death induced by ultraviolet C (UVC), which causes DNA damage. The small heat shock protein αB-crystallin (αBC) is identified as a MG23 binding molecule and its knockdown facilitates death of UVC-exposed cells. Conversely, αBC lowered UVC sensitivity when expressed as an ER-anchored form. Taken together, the results suggest that MG23 plays a protective role against UVC by accumulating αBC in the close vicinity of the ER.
Related Concept Videos
Nucleotide Excision Repair
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
Nucleotide Excision Repair
Export of Misfolded Proteins out of the ER
The Unfolded Protein Response
Regulation of the Unfolded Protein Response
Mutations
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...

