This entry represents the MCU family, whose members include MCU and MCUb from mammals and MCU1-6 from Arabidopsis. MCU is a mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria [, , ]. MCUb negatively regulates the activity of MCU [].
Essential MCU regulator (EMRE) is a component of the mitochondrial calcium uniporter complex in metazoa, a complex that mediates calcium uptake into mitochondria. It bridges the calcium-sensing components of the complex, MICU1 and MICU2, and the pore-forming subunit MCU, and it is essential for the complex uniporter activity [].
This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1 [, , ]. A study in mammals and in yeast homologue fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU [], however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU [, ]. The role of CCDC90B proteins is still not known.
This entry represents the C-terminal domain of MCU, which is a mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria [, , ]. This domain can also be found in MCUb, which negatively regulates the activity of MCU [].
Mitochondrial calcium uniporter regulator 1 (MCUR1), also known as CCDC90A, is a key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion. It plays a direct role in uniporter-mediated calcium uptake, possibly via a direct interaction with MCU [, , ].
This entry represents a group of calcium uptake proteins, including MICU1/2/3 from humans. They contain the conserved EF-hand Ca2+-binding domains. MICU1 and MICU2 are the main regulators of the mitochondrial Ca(2+)-uniporter (MCU) []. MICU2 forms a heterodimer with MICU1 to modulate MCU channel activity []. MICU3 a tissue-specific enhancer of mitochondrial calcium uptake [].