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Volumn 8, Issue 6, 2015, Pages 1-5

The evolution of MICOS: Ancestral and derived functions and interactions

Author keywords

Evolutionary cell biology; MCS; Membrane contact sites; MICOS; Mitofilin

Indexed keywords


EID: 84958550382     PISSN: None     EISSN: 19420889     Source Type: Journal    
DOI: 10.1080/19420889.2015.1094593     Document Type: Article
Times cited : (35)

References (45)
  • 1
    • 33745737928 scopus 로고    scopus 로고
    • Structure and dynamics of the mitochondrial inner membrane cristae
    • PMID:16730811
    • Mannella CA. Structure and dynamics of the mitochondrial inner membrane cristae. Biochim Biophys Acta 2006; 1763:542-8; PMID:16730811; http://dx.doi.org/10.1016/j.bbamcr.2006.04.006
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 542-548
    • Mannella, C.A.1
  • 2
    • 84878703165 scopus 로고    scopus 로고
    • The connection between inner membrane topology and mitochondrial function
    • Mannella CA, Lederer WJ, Jafri MS. The connection between inner membrane topology and mitochondrial function. J Mol Cell Cardiol 2013; 62C:51-7; http://dx.doi.org/10.1016/j.yjmcc.2013.05.001
    • (2013) J Mol Cell Cardiol , vol.62C , pp. 51-57
    • Mannella, C.A.1    Lederer, W.J.2    Jafri, M.S.3
  • 6
    • 80054772036 scopus 로고    scopus 로고
    • MINOS is plus: A Mitofilin complex for mitochondrial membrane contacts
    • PMID:22014515
    • Herrmann JM. MINOS is plus: a Mitofilin complex for mitochondrial membrane contacts. Dev Cell 2011; 21:599-600; PMID:22014515; http://dx.doi.org/10.1016/j.devcel.2011.09.013
    • (2011) Dev Cell , vol.21 , pp. 599-600
    • Herrmann, J.M.1
  • 8
    • 84869422571 scopus 로고    scopus 로고
    • Mitofilin complexes: Conserved organizers of mitochondrial membrane architecture
    • PMID:23109542
    • Zerbes RM, van der Klei IJ, Veenhuis M, Pfanner N, van der Laan M, Bohnert M. Mitofilin complexes: conserved organizers of mitochondrial membrane architecture. Biol Chem 2012; 393:1247-61; PMID:23109542; http://dx. doi.org/10.1515/hsz-2012-0239
    • (2012) Biol Chem , vol.393 , pp. 1247-1261
    • Zerbes, R.M.1    Van Der Klei, I.J.2    Veenhuis, M.3    Pfanner, N.4    Van Der Laan, M.5    Bohnert, M.6
  • 9
    • 84930926530 scopus 로고    scopus 로고
    • Ancient Homology of the Mitochondrial Contact Site and Cristae Organizing System Points to an Endosymbiotic Origin of Mitochondrial Cristae
    • Muñoz-Gómez SA, Slamovits CH, Dacks JB, Baier KA, Spencer KD, Wideman JG. Ancient Homology of the Mitochondrial Contact Site and Cristae Organizing System Points to an Endosymbiotic Origin of Mitochondrial Cristae. Curr Biol 2015; 25:1489-95; http://dx.doi.org/10.1016/j.cub.2015.04.006
    • (2015) Curr Biol , vol.25 , pp. 1489-1495
    • Muñoz-Gómez, S.A.1    Slamovits, C.H.2    Dacks, J.B.3    Baier, K.A.4    Spencer, K.D.5    Wideman, J.G.6
  • 11
    • 84855874566 scopus 로고    scopus 로고
    • MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization
    • PMID:22114354
    • Alkhaja AK, Jans DC, Nikolov M, Vukotic M, Lytovchenko O, Ludewig F, Schliebs W, Riedel D, Urlaub H, Jakobs S, et al. MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization. Mol Biol Cell 2012; 23:247-57; PMID:22114354; http://dx.doi.org/10.1091/mbc.E11-09-0774
    • (2012) Mol Biol Cell , vol.23 , pp. 247-257
    • Alkhaja, A.K.1    Jans, D.C.2    Nikolov, M.3    Vukotic, M.4    Lytovchenko, O.5    Ludewig, F.6    Schliebs, W.7    Riedel, D.8    Urlaub, H.9    Jakobs, S.10
  • 12
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • PMID:17043137
    • Vogel F, Bornhövd C, Neupert W, Reichert AS. Dynamic subcompartmentalization of the mitochondrial inner membrane. J Cell Biol 2006; 175:237-47; PMID:17043137; http://dx.doi.org/10.1083/jcb.200605138
    • (2006) J Cell Biol , vol.175 , pp. 237-247
    • Vogel, F.1    Bornhövd, C.2    Neupert, W.3    Reichert, A.S.4
  • 13
    • 56349166020 scopus 로고    scopus 로고
    • Cristae formation-linking ultrastructure and function of mitochondria
    • PMID:18620004
    • Zick M, Rabl R, Reichert AS. Cristae formation-linking ultrastructure and function of mitochondria. Biochim Biophys Acta 2009; 1793:5-19; PMID:18620004; http://dx.doi.org/10.1016/j.bbamcr.2008.06.013
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 5-19
    • Zick, M.1    Rabl, R.2    Reichert, A.S.3
  • 16
    • 85018214596 scopus 로고    scopus 로고
    • Mic10 Oligomerization Pinches off Mitochondrial Cristae
    • PMID:25955201
    • Milenkovic D, Larsson NG. Mic10 Oligomerization Pinches off Mitochondrial Cristae. Cell Metab 2015; 21:660-1; PMID:25955201; http://dx.doi.org/10.1016/j. cmet.2015.04.020
    • (2015) Cell Metab , vol.21 , pp. 660-661
    • Milenkovic, D.1    Larsson, N.G.2
  • 17
    • 84945913593 scopus 로고    scopus 로고
    • Meinecke M.Mic10 Oligomerizes to Bend Mitochondrial Inner Membranes at Cristae Junctions
    • PMID:25955211
    • Barbot M, Jans DC, Schulz C, Denkert N, Kroppen B, Hoppert M, Jakobs S, Meinecke M.Mic10 Oligomerizes to Bend Mitochondrial Inner Membranes at Cristae Junctions. Cell Metab 2015; 21:756-63; PMID:25955211; http://dx.doi.org/10.1016/j.cmet.2015.04.006
    • (2015) Cell Metab , vol.21 , pp. 756-763
    • Barbot, M.1    Jans, D.C.2    Schulz, C.3    Denkert, N.4    Kroppen, B.5    Hoppert, M.6    Jakobs, S.7
  • 19
    • 84877966571 scopus 로고    scopus 로고
    • APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria
    • PMID:23704930
    • Weber TA, Koob S, Heide H, Wittig I, Head B, van der Bliek A, Brandt U, Mittelbronn M, Reichert AS. APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria. PloS One 2013; 8:e63683; PMID:23704930; http://dx.doi.org/10.1371/journal.pone.0063683
    • (2013) Plos One , vol.8
    • Weber, T.A.1    Koob, S.2    Heide, H.3    Wittig, I.4    Head, B.5    Van Der Bliek, A.6    Brandt, U.7    Mittelbronn, M.8    Reichert, A.S.9
  • 20
    • 84922394075 scopus 로고    scopus 로고
    • Novel intracellular functions of apolipoproteins: The ApoO protein family as constituents of the Mitofilin/MINOS complex determines cristae morphology in mitochondria
    • PMID:24391192
    • Koob S, Reichert AS. Novel intracellular functions of apolipoproteins: the ApoO protein family as constituents of the Mitofilin/MINOS complex determines cristae morphology in mitochondria. Biol Chem 2014; 395:285-96; PMID:24391192; http://dx.doi.org/10.1515/hsz-2013-0274
    • (2014) Biol Chem , vol.395 , pp. 285-296
    • Koob, S.1    Reichert, A.S.2
  • 21
    • 84929154199 scopus 로고    scopus 로고
    • MICOS coordinates with respiratory complexes and lipids to establish mitochondrial inner membrane architecture
    • Friedman JR, Mourier A, Yamada J, McCaffery JM, Nunnari J. MICOS coordinates with respiratory complexes and lipids to establish mitochondrial inner membrane architecture. Elife 2015; 4:e07739; http://dx.doi.org/10.7554/eLife.07739
    • (2015) Elife , vol.4
    • Friedman, J.R.1    Mourier, A.2    Yamada, J.3    McCaffery, J.M.4    Nunnari, J.5
  • 22
    • 84924956420 scopus 로고    scopus 로고
    • Detailed Analysis of the Human Mitochondrial Contact Site Complex Indicate a Hierarchy of Subunits
    • PMID: 25781180
    • Ott C, Dorsch E, Fraunholz M, Straub S, Kozjak- Pavlovic V. Detailed Analysis of the Human Mitochondrial Contact Site Complex Indicate a Hierarchy of Subunits. PLoS One 2015; 10:e0120213; PMID: 25781180; http://dx.doi.org/10.1371/journal.pone.0- 120213
    • (2015) Plos One , vol.10
    • Ott, C.1    Dorsch, E.2    Fraunholz, M.3    Straub, S.4    Kozjak- Pavlovic, V.5
  • 23
    • 84857869559 scopus 로고    scopus 로고
    • Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes
    • PMID:22252321
    • Ott C, Ross K, Straub S, Thiede B, Götz M, Goosmann C, Krischke M, Mueller MJ, Krohne G, Rudel T, et al. Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes. Mol Cell Biol 2012; 32:1173-88; PMID:22252321; http://dx. doi.org/10.1128/MCB.06388-11
    • (2012) Mol Cell Biol , vol.32 , pp. 1173-1188
    • Ott, C.1    Ross, K.2    Straub, S.3    Thiede, B.4    Götz, M.5    Goosmann, C.6    Krischke, M.7    Mueller, M.J.8    Krohne, G.9    Rudel, T.10
  • 24
    • 84861673870 scopus 로고    scopus 로고
    • The C-terminal domain of Fcj1 is required for formation of crista junctions and interacts with the TOB/SAM complex in mitochondria
    • PMID:22496419
    • Körner C, Barrera M, Dukanovic J, Eydt K, Harner M, Rabl R, Vogel F, Rapaport D, Neupert W, Reichert AS. The C-terminal domain of Fcj1 is required for formation of crista junctions and interacts with the TOB/SAM complex in mitochondria. Mol Biol Cell 2012; 23:2143-55; PMID:22496419; http://dx.doi.org/10.1091/mbc.E11-10-0831
    • (2012) Mol Biol Cell , vol.23 , pp. 2143-2155
    • Körner, C.1    Barrera, M.2    Dukanovic, J.3    Eydt, K.4    Harner, M.5    Rabl, R.6    Vogel, F.7    Rapaport, D.8    Neupert, W.9    Reichert, A.S.10
  • 25
    • 84864843177 scopus 로고    scopus 로고
    • Role of MINOS in mitochondrial membrane architecture: Cristae morphology and outer membrane interactions differentially depend on mitofilin domains
    • PMID:22575891
    • Zerbes RM, Bohnert M, Stroud DA, von der Malsburg K, Kram A, Oeljeklaus S, Warscheid B, Becker T, Wiedemann N, Veenhuis M, et al. Role of MINOS in mitochondrial membrane architecture: cristae morphology and outer membrane interactions differentially depend on mitofilin domains. J Mol Biol 2012; 422:183-91; PMID:22575891; http://dx.doi.org/10.1016/j.jmb.2012.05.004
    • (2012) J Mol Biol , vol.422 , pp. 183-191
    • Zerbes, R.M.1    Bohnert, M.2    Stroud, D.A.3    Von Der Malsburg, K.4    Kram, A.5    Oeljeklaus, S.6    Warscheid, B.7    Becker, T.8    Wiedemann, N.9    Veenhuis, M.10
  • 27
    • 84859265052 scopus 로고    scopus 로고
    • Role of MINOS in mitochondrial membrane architecture and biogenesis
    • PMID:22386790
    • van der Laan M, Bohnert M, Wiedemann N, Pfanner N. Role of MINOS in mitochondrial membrane architecture and biogenesis. Trends Cell Biol 2012; 22:185-92; PMID:22386790; http://dx.doi.org/10.1016/j.tcb.2012.01.004
    • (2012) Trends Cell Biol , vol.22 , pp. 185-192
    • Van Der Laan, M.1    Bohnert, M.2    Wiedemann, N.3    Pfanner, N.4
  • 28
    • 34447268008 scopus 로고    scopus 로고
    • The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC 11
    • PMID:17624330
    • Xie J, Marusich MF, Souda P, Whitelegge J, Capaldi RA. The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC 11. FEBS Lett 2007; 581:3545-9; PMID:17624330; http://dx.doi.org/10.1016/j.febslet.2007.06.052
    • (2007) FEBS Lett , vol.581 , pp. 3545-3549
    • Xie, J.1    Marusich, M.F.2    Souda, P.3    Whitelegge, J.4    Capaldi, R.A.5
  • 29
    • 78049249511 scopus 로고    scopus 로고
    • Disrupted-inschizophrenia 1 (DISC1) plays essential roles in mitochondria in collaboration with Mitofilin
    • PMID:20880836
    • Park YU, Jeong J, Lee H, Mun JY, Kim JH, Lee JS, Nguyen MD, Han SS, Suh PG, Park SK. Disrupted-inschizophrenia 1 (DISC1) plays essential roles in mitochondria in collaboration with Mitofilin. Proc Natl Acad Sci USA 2010; 107:17785-90; PMID:20880836; http://dx.doi.org/10.1073/pnas.1004361107
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17785-17790
    • Park, Y.U.1    Jeong, J.2    Lee, H.3    Mun, J.Y.4    Kim, J.H.5    Lee, J.S.6    Nguyen, M.D.7    Han, S.S.8    Suh, P.G.9    Park, S.K.10
  • 31
    • 84898463186 scopus 로고    scopus 로고
    • Aim24 and MICOS modulate respiratory function, tafazzin-related cardiolipin modification and mitochondrial architecture
    • PMID:24714493
    • Harner ME, Unger A-K, Izawa T, Walther DM, Özbalci C, Geimer S, Reggiori F, Brügger B, Mann M, Westermann B, et al. Aim24 and MICOS modulate respiratory function, tafazzin-related cardiolipin modification and mitochondrial architecture. Elife 2014; 3:e01684; PMID:24714493; http://dx.doi.org/10.7554/eLife.01684
    • (2014) Elife , vol.3
    • Harner, M.E.1    Unger, A.-K.2    Izawa, T.3    Walther, D.M.4    Özbalci, C.5    Geimer, S.6    Reggiori, F.7    Brügger, B.8    Mann, M.9    Westermann, B.10
  • 32
    • 84931274643 scopus 로고    scopus 로고
    • Cox17 is an auxiliary factor involved in the control of the mitochondrial contact site and cristae organizing system
    • PMID:25918166
    • Chojnacka M, Gornicka A, Oeljeklaus S, Warscheid B, Chacinska A. Cox17 is an auxiliary factor involved in the control of the mitochondrial contact site and cristae organizing system. J Biol Chem 2015; 290:15304-12; PMID:25918166; http://dx.doi.org/10.1074/jbc.M115.645069
    • (2015) J Biol Chem , vol.290 , pp. 15304-15312
    • Chojnacka, M.1    Gornicka, A.2    Oeljeklaus, S.3    Warscheid, B.4    Chacinska, A.5
  • 33
    • 84883233522 scopus 로고    scopus 로고
    • The Ancient and Widespread Nature of the ER– Mitochondria Encounter Structure
    • PMID:23813918
    • Wideman JG, Gawryluk RMR, Gray MW, Dacks JB. The Ancient and Widespread Nature of the ER– Mitochondria Encounter Structure. Mol Biol Evol 2013; 30:2044-9; PMID:23813918; http://dx.doi.org/10.1093/molbev/mst120
    • (2013) Mol Biol Evol , vol.30 , pp. 2044-2049
    • Wideman, J.G.1    Gawryluk, R.2    Gray, M.W.3    Dacks, J.B.4
  • 35
    • 0037428132 scopus 로고    scopus 로고
    • Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly
    • PMID:12522254
    • Voulhoux R, Bos MP, Geurtsen J, Mols M, Tommassen J. Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly. Science 2003; 299:262-5; PMID:12522254; http://dx.doi.org/10.1126/science.1078973
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 36
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the Molecular Machines for Protein Import into Mitochondria
    • PMID: 16857931
    • Dolezal P, Likic V, Tachezy J, Lithgow T. Evolution of the Molecular Machines for Protein Import into Mitochondria. Science 2006; 313:314-8; PMID: 16857931; http://dx.doi.org/10.1126/science.1127895
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 37
    • 84856853161 scopus 로고    scopus 로고
    • Mitochondrial Disulfide Relay: Redox-regulated Protein Import into the Intermembrane Space
    • PMID:22157015
    • Herrmann JM, Riemer J.: Mitochondrial Disulfide Relay: Redox-regulated Protein Import into the Intermembrane Space. J Biol Chem 2012; 287:4426-33; PMID:22157015; http://dx.doi.org/10.1074/jbc. R111.270678
    • (2012) J Biol Chem , vol.287 , pp. 4426-4433
    • Herrmann, J.M.1    Riemer, J.2
  • 38
    • 84871714058 scopus 로고    scopus 로고
    • Loss, replacement and gain of proteins at the origin of the mitochondria
    • Huynen MA, Duarte I, Szklarczyk R. Loss, replacement and gain of proteins at the origin of the mitochondria. Biochim Biophys Acta BBA - Bioenerg 2013; 1827:224-31; http://dx.doi.org/10.1016/j.bbabio.2012.08.001
    • (2013) Biochim Biophys Acta BBA - Bioenerg , vol.1827 , pp. 224-231
    • Huynen, M.A.1    Duarte, I.2    Szklarczyk, R.3
  • 41
    • 84924232481 scopus 로고    scopus 로고
    • Perspective on Transport of Proteins into Mitochondria: A Myriad of Open Questions
    • PMID:25676309
    • Neupert W. A Perspective on Transport of Proteins into Mitochondria: A Myriad of Open Questions. J Mol Biol 2015; 427:1135-58; PMID:25676309; http://dx.doi.org/10.1016/j.jmb.2015.02.001
    • (2015) J Mol Biol , vol.427 , pp. 1135-1158
    • Neupert, W.A.1
  • 42
    • 84897015575 scopus 로고    scopus 로고
    • Integrating mitochondrial organization and dynamics with cellular architecture
    • PMID:24529244
    • Jayashankar V, Rafelski SM. Integrating mitochondrial organization and dynamics with cellular architecture. Curr Opin Cell Biol 2014; 26:34-40; PMID:24529244; http://dx.doi.org/10.1016/j.ceb.2013.09.002
    • (2014) Curr Opin Cell Biol , vol.26 , pp. 34-40
    • Jayashankar, V.1    Rafelski, S.M.2
  • 44
    • 84862839039 scopus 로고    scopus 로고
    • The Evolution of Multimeric Protein Assemblages
    • PMID:22144639
    • Lynch M. The Evolution of Multimeric Protein Assemblages. Mol Biol Evol 2012; 29:1353-66; PMID:22144639; http://dx.doi.org/10.1093/molbev/msr300
    • (2012) Mol Biol Evol , vol.29 , pp. 1353-1366
    • Lynch, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.