{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tomar D"],"funding":["NIDA NIH HHS","NCRR NIH HHS","NIDDK NIH HHS","NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["1673-85"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4880542"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(8)"],"pubmed_abstract":["Mitochondrial Ca(2+) Uniporter (MCU)-dependent mitochondrial Ca(2+) uptake is the primary mechanism for increasing matrix Ca(2+) in most cell types. However, a limited understanding of the MCU complex assembly impedes the comprehension of the precise mechanisms underlying MCU activity. Here, we report that mouse cardiomyocytes and endothelial cells lacking MCU regulator 1 (MCUR1) have severely impaired [Ca(2+)]m uptake and IMCU current. MCUR1 binds to MCU and EMRE and function as a scaffold factor. Our protein binding analyses identified the minimal, highly conserved regions of coiled-coil domain of both MCU and MCUR1 that are necessary for heterooligomeric complex formation. Loss of MCUR1 perturbed MCU heterooligomeric complex and functions as a scaffold factor for the assembly of MCU com"],"journal":["Cell reports"],"pubmed_title":["MCUR1 Is a Scaffold Factor for the MCU Complex Function and Promotes Mitochondrial Bioenergetics."],"pmcid":["PMC4880542"],"funding_grant_id":["P01 HL091799","R01 HL123966","R01 HL086699","P20 GM103446","S10 RR027327","P30 DK019525","P01 DA037830","R01 HL119306","R01 GM111672","R01 GM109882"],"pubmed_authors":["Huang J","Rabinowitz JE","Ahima RS","Dong Z","Cutri AR","Barrero C","Gohil VM","Luongo TS","Rajan S","Koch DA","Breves SL","Schumacher SM","Houser SR","Shanmughapriya S","Madesh M","Thomas T","Cheung JY","Timbalia SA","Goldman SJ","Stathopulos P","Jana F","Tomar D","Corbally DP","Rockman ME","Elrod JW","Dietrich A","Koch WJ","Patel V","Song J","Nemani N","Fairweather JP","Hoffman NE","Merali S","Zhang X","Caplan J"],"additional_accession":[]},"is_claimable":false,"name":"MCUR1 Is a Scaffold Factor for the MCU Complex Function and Promotes Mitochondrial Bioenergetics.","description":"Mitochondrial Ca(2+) Uniporter (MCU)-dependent mitochondrial Ca(2+) uptake is the primary mechanism for increasing matrix Ca(2+) in most cell types. However, a limited understanding of the MCU complex assembly impedes the comprehension of the precise mechanisms underlying MCU activity. Here, we report that mouse cardiomyocytes and endothelial cells lacking MCU regulator 1 (MCUR1) have severely impaired [Ca(2+)]m uptake and IMCU current. MCUR1 binds to MCU and EMRE and function as a scaffold factor. Our protein binding analyses identified the minimal, highly conserved regions of coiled-coil domain of both MCU and MCUR1 that are necessary for heterooligomeric complex formation. Loss of MCUR1 perturbed MCU heterooligomeric complex and functions as a scaffold factor for the assembly of MCU com","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 May","modification":"2025-04-04T02:35:39.433Z","creation":"2019-03-27T02:14:34Z"},"accession":"S-EPMC4880542","cross_references":{"pubmed":["27184846"],"doi":["10.1016/j.celrep.2016.04.050"]}}