Structure and function of the N-terminal domain of the human mitochondrial calcium uniporter

نویسندگان

  • Youngjin Lee
  • Choon Kee Min
  • Tae Gyun Kim
  • Hong Ki Song
  • Yunki Lim
  • Dongwook Kim
  • Kahee Shin
  • Moonkyung Kang
  • Jung Youn Kang
  • Hyung-Seop Youn
  • Jung-Gyu Lee
  • Jun Yop An
  • Kyoung Ryoung Park
  • Jia Jia Lim
  • Ji Hun Kim
  • Ji Hye Kim
  • Zee Yong Park
  • Yeon-Soo Kim
  • Jimin Wang
  • Do Han Kim
  • Soo Hyun Eom
چکیده

The mitochondrial calcium uniporter (MCU) is responsible for mitochondrial calcium uptake and homeostasis. It is also a target for the regulation of cellular anti-/pro-apoptosis and necrosis by several oncogenes and tumour suppressors. Herein, we report the crystal structure of the MCU N-terminal domain (NTD) at a resolution of 1.50 Å in a novel fold and the S92A MCU mutant at 2.75 Å resolution; the residue S92 is a predicted CaMKII phosphorylation site. The assembly of the mitochondrial calcium uniporter complex (uniplex) and the interaction with the MCU regulators such as the mitochondrial calcium uptake-1 and mitochondrial calcium uptake-2 proteins (MICU1 and MICU2) are not affected by the deletion of MCU NTD. However, the expression of the S92A mutant or a NTD deletion mutant failed to restore mitochondrial Ca(2+) uptake in a stable MCU knockdown HeLa cell line and exerted dominant-negative effects in the wild-type MCU-expressing cell line. These results suggest that the NTD of MCU is essential for the modulation of MCU function, although it does not affect the uniplex formation.

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عنوان ژورنال:

دوره 16  شماره 

صفحات  -

تاریخ انتشار 2015