EMRE is an essential component of the mitochondrial calcium uniporter complex.

Science
Authors
Keywords
Abstract

The mitochondrial uniporter is a highly selective calcium channel in the organelle's inner membrane. Its molecular components include the EF-hand-containing calcium-binding proteins mitochondrial calcium uptake 1 (MICU1) and MICU2 and the pore-forming subunit mitochondrial calcium uniporter (MCU). We sought to achieve a full molecular characterization of the uniporter holocomplex (uniplex). Quantitative mass spectrometry of affinity-purified uniplex recovered MICU1 and MICU2, MCU and its paralog MCUb, and essential MCU regulator (EMRE), a previously uncharacterized protein. EMRE is a 10-kilodalton, metazoan-specific protein with a single transmembrane domain. In its absence, uniporter channel activity was lost despite intact MCU expression and oligomerization. EMRE was required for the interaction of MCU with MICU1 and MICU2. Hence, EMRE is essential for in vivo uniporter current and additionally bridges the calcium-sensing role of MICU1 and MICU2 with the calcium-conducting role of MCU.

Year of Publication
2013
Journal
Science
Volume
342
Issue
6164
Pages
1379-82
Date Published
2013 Dec 13
ISSN
1095-9203
URL
DOI
10.1126/science.1242993
PubMed ID
24231807
PubMed Central ID
PMC4091629
Links
Grant list
F32HL107021 / HL / NHLBI NIH HHS / United States
R24 DK080261 / DK / NIDDK NIH HHS / United States
P30 HD018655 / HD / NICHD NIH HHS / United States
F32 HL107021 / HL / NHLBI NIH HHS / United States
Howard Hughes Medical Institute / United States
DK080261 / DK / NIDDK NIH HHS / United States