[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki40\/mitochondrial-dynamics-protein-mid49-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki40\/mitochondrial-dynamics-protein-mid49-wikipedia\/","headline":"Mitochondrial dynamics protein MID49 – Wikipedia","name":"Mitochondrial dynamics protein MID49 – Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens Mitochondrial elongation factor 2 is a protein that","datePublished":"2014-07-21","dateModified":"2014-07-21","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki40\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki40\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki40\/mitochondrial-dynamics-protein-mid49-wikipedia\/","wordCount":4098,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiensMitochondrial elongation factor 2 is a protein that in humans is encoded by the MIEF2 gene.[5]Table of ContentsMID49 Protein Structure[edit]MID49 Protein’s Role in Mitochondrial Binary Fission[edit]Function[edit]References[edit]Further reading[edit]MID49 Protein Structure[edit]The MID49 protein is used to assist in mitochondrial binary fission. It is a dynamic peripheral protein receptor found on the surface of the mitochondrial membrane. MID51 is a very similar protein and studies have shown that it has a variant nucleotidyl transferase structure which allows it to move phosphates as a co-factor. This structure and ability is essential because it allows it to interact with ADP which will activate the Drp1 protein. Further studies have shown that MID49 and MID51 are homologous in sequence and MID49 also has a nucleotidyl transferase domain but it is still unknown if MID49 can also bind a co-factor. Instead of a co-factor ligand, it was found that MID49 has a loop structure on its surface that allows it to physically interact with the Drp1 protein. To recap, the MID51 and MID49 are both similar proteins that recruit Drp1 protein to induce mitochondrial binary fission but they have small differences in structure which allows them to bind Drp1 in different ways.[6]MID49 Protein’s Role in Mitochondrial Binary Fission[edit]The MID49 peripheral protein will attract the Drp1 to the surface of the mitochondrial membrane which then induces endoplasmic reticulum contact. The ER then releases Ca2+ into the mitochondria once there is physical contact at the membrane. The influx of calcium induces a constriction response in the mitochondria. With this constriction in the middle, the MID49 keeps recruiting more and more Drp1 proteins to make a sort of chain structure to wrap around that narrowed area called the oligomeric ring. The Drp1 proteins will eventually disassociate with the MID49 proteins through hydrolysis which causes a much tighter constriction around the mitochondria. There are still studies being done to confirm if this constriction alone will then split the mitochondria in the middle to complete a binary fission event.[7]Function[edit]This gene encodes an outer mitochondrial membrane protein that functions in the regulation of mitochondrial morphology. It can directly recruit the fission mediator dynamin-related protein 1 (Drp1) to the mitochondrial surface. The gene is located within the Smith-Magenis syndrome region on chromosome 17. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jun 2011].References[edit]^ a b c ENSG00000177427 GRCh38: Ensembl release 89: ENSG00000284495, ENSG00000177427 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018599 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Entrez Gene: Mitochondrial elongation factor 2”. Retrieved 2018-04-01.^ Los\u00f3n, Oliver C; Meng, Shuxia; Ngo, Huu; Liu, Raymond; Kaiser, Jens T; Chan, David C (March 2015). “Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1”. Protein Science. 24 (3): 386\u2013394. doi:10.1002\/pro.2629. ISSN\u00a00961-8368. PMC\u00a04353364. PMID\u00a025581164.^ Fenton, Adam R.; Jongens, Thomas A.; Holzbaur, Erika L. F. (2021-02-01). “Mitochondrial dynamics: Shaping and remodeling an organelle network”. Current Opinion in Cell Biology. Cell Architecture. 68: 28\u201336. doi:10.1016\/j.ceb.2020.08.014. ISSN\u00a00955-0674. PMC\u00a07925334. PMID\u00a032961383.(Updated 2 and 3 reference list)2. Los\u00f3n, Oliver C; Meng, Shuxia; Ngo, Huu; Liu, Raymond; Kaiser, Jens T; Chan, David C (2015-3). “Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1”. Protein Science.3. Fenton, Adam R.; Jongens, Thomas A.; Holzbaur, Erika L. F. (2021-02-01). “Mitochondrial dynamics: Shaping and remodeling an organelle network”. Current Opinion in Cell Biology. Cell Architecture. 68: 28\u201336.Further reading[edit]Sarimski K (2004). “Communicative competence and behavioural phenotype in children with Smith-Magenis syndrome”. Genet. Couns. 15 (3): 347\u201355. PMID\u00a015517828.Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT (June 2011). “MiD49 and MiD51, new components of the mitochondrial fission machinery”. EMBO Rep. 12 (6): 565\u201373. doi:10.1038\/embor.2011.54. PMC\u00a03128275. PMID\u00a021508961.Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT (June 2011). “MiD49 and MiD51, new components of the mitochondrial fission machinery”. EMBO Rep. 12 (6): 565\u201373. doi:10.1038\/embor.2011.54. PMC\u00a03128275. PMID\u00a021508961.Los\u00f3n OC, Song Z, Chen H, Chan DC (March 2013). “Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission”. Mol. Biol. Cell. 24 (5): 659\u201367. doi:10.1091\/mbc.E12-10-0721. PMC\u00a03583668. PMID\u00a023283981.Liu T, Yu R, Jin SB, Han L, Lendahl U, Zhao J, Nist\u00e9r M (November 2013). “The mitochondrial elongation factors MIEF1 and MIEF2 exert partially distinct functions in mitochondrial dynamics”. Exp. Cell Res. 319 (18): 2893\u2013904. doi:10.1016\/j.yexcr.2013.07.010. PMID\u00a023880462.Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT (September 2013). “Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission”. J. Biol. Chem. 288 (38): 27584\u201393. doi:10.1074\/jbc.M113.479873. PMC\u00a03779755. PMID\u00a023921378.Xu S, Cherok E, Das S, Li S, Roelofs BA, Ge SX, Polster BM, Boyman L, Lederer WJ, Wang C, Karbowski M (January 2016). “Mitochondrial E3 ubiquitin ligase MARCH5 controls mitochondrial fission and cell sensitivity to stress-induced apoptosis through regulation of MiD49 protein”. Mol. Biol. Cell. 27 (2): 349\u201359. doi:10.1091\/mbc.E15-09-0678. PMC\u00a04713136. PMID\u00a026564796.Otera H, Miyata N, Kuge O, Mihara K (February 2016). “Drp1-dependent mitochondrial fission via MiD49\/51 is essential for apoptotic cristae remodeling”. J. Cell Biol. 212 (5): 531\u201344. doi:10.1083\/jcb.201508099. PMC\u00a04772499. PMID\u00a026903540.Atkins K, Dasgupta A, Chen KH, Mewburn J, Archer SL (November 2016). “The role of Drp1 adaptor proteins MiD49 and MiD51 in mitochondrial fission: implications for human disease”. Clin. Sci. 130 (21): 1861\u201374. doi:10.1042\/CS20160030. PMID\u00a027660309.This article incorporates text from the United States National Library of Medicine, which is in the public domain."},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki40\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki40\/mitochondrial-dynamics-protein-mid49-wikipedia\/#breadcrumbitem","name":"Mitochondrial dynamics protein MID49 – Wikipedia"}}]}]