ID 109894
Title Transcription
UCP3 ト Hax-1 ノ ソウゴ サヨウ ニヨル ミトコンドリア ノ カルシウム ノ ウド ノ チョウセツ
Title Alternative
The interaction between uncoupling protein3 and Hax-1 is regulated by calcium ion in mitochondria
Author
Haruna, Marie Department of Nutritional Physiology, Institute of Health Biosciences, University of Tokushima
Hirasaka, Katsuya Graduate School of Fisheries Science and Enviromental Studies, Nagasaki University
Tomita, Chisato Department of Nutritional Physiology, Institute of Health Biosciences, University of Tokushima
Abe, Tomoki Department of Nutritional Physiology, Institute of Health Biosciences, University of Tokushima KAKEN Search Researchers
Ohno, Ayako Department of Nutritional Physiology, Institute of Health Biosciences, University of Tokushima
Teshima-Kondo, Shigetada Department of Nutritional Physiology, Institute of Health Biosciences, University of Tokushima KAKEN Search Researchers
Nikawa, Takeshi Department of Nutritional Physiology, Institute of Health Biosciences, University of Tokushima Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Keywords
mitochondria
calcium ion
Content Type
Journal Article
Description
Mitochondrial Ca2+ plays an important role in the regulations of various cellular functions. Uncoupling protein 3 (UCP3) is primarily expressed in the inner membrane of skeletal muscle mitochondria. Recently, it has been reported that UCP3 is associated with Ca2+ uptake into mitochondria. However, the mechanisms by which UCP3 regulates mitochondrial Ca2+ uptake are not well understood. Here we report that UCP3interacts with HS‐1associated protein X‐1 (Hax‐1), an anti-apoptotic protein that is localized in mitochondria, which is involved in cellular responses to Ca2+. The hydrophilic sequences within the loop2, matrix-localized hydrophilic domain of mouse UCP3are necessary for binding to Hax‐1of the C-terminal domain in adjacent to mitochondrial innermembrane. Interestingly, interaction of these proteins occurs the calciumdependent manner. Moreover, NMR spectrum of the C-terminal domain of Hax‐1was dramatically changed by removal of Ca2+, suggesting that the C-terminal domain of Hax‐1 underwent a Ca2+-induced conformation change. In the Ca2+-free states, C-terminal Hax‐1 didn’t change the structure, suggesting that Ca2+ binding may induce the change of protein structure of Hax‐1 C-terminus. These studies identify a novel UCP3‐Hax‐1complex regulates the influx of Ca2+ into mitochondria. Thus, the efficacy of UCP3‐Hax‐1in mitochondrial calcium regulation may provide a novel therapeutic approach against mitochondrial dysfunction-related disease.
Journal Title
四国医学雑誌
ISSN
00373699
NCID
AN00102041
Publisher
徳島医学会
Volume
70
Issue
5-6
Start Page
149
End Page
154
Sort Key
149
Published Date
2014-12-25
Remark
P.149著者名日本語表記では「真板 綾子」となっているが、P.154英語表記では「Ayako Ohno」となっている。
FullText File
language
jpn
TextVersion
Publisher
departments
Medical Sciences