mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells
Mitochondria are dynamic organelles that change morphology by controlled fission and fusion events. Mitochondrial fission is regulated by a conserved protein complex assembled at the outer membrane. Human MTP18 is a novel nuclear-encoded mitochondrial membrane protein, implicated in controlling mito...
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| Veröffentlicht in: | Journal of cell science 2005-07, Vol.118 (14), p.3049-3059 |
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| container_issue | 14 |
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| container_title | Journal of cell science |
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| creator | Tondera, Daniel Czauderna, Frank Paulick, Katharina Schwarzer, Rolf Kaufmann, Jörg Santel, Ansgar |
| description | Mitochondria are dynamic organelles that change morphology by controlled fission and fusion events. Mitochondrial fission is regulated by a conserved protein complex assembled at the outer membrane. Human MTP18 is a novel nuclear-encoded mitochondrial membrane protein, implicated in controlling mitochondrial fission. Upon overexpression of MTP18, mitochondrial morphology was altered from filamentous to punctate structures suggesting excessive mitochondrial fission. Mitochondrial fragmentation was blocked in cells coexpressing either the mitochondrial fusion protein Mfn1 or Drp1[superscript K38A], a dominant negative version of the fission protein Drp1. Also, a loss-of function of endogenous MTP18 by RNA interference (RNAi) resulted in highly fused mitochondria. Moreover, MTP18 appears to be required for mitochondrial fission because it is blocked after overexpression of hFis1 in cells with RNAi-mediated MTP18 knockdown. In conclusion, we propose that MTP18 functions as an essential intramitochondrial component of the mitochondrial division apparatus, contributing to the maintenance of mitochondrial morphology. |
| doi_str_mv | 10.1242/jcs.02415 |
| format | Article |
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Mitochondrial fission is regulated by a conserved protein complex assembled at the outer membrane. Human MTP18 is a novel nuclear-encoded mitochondrial membrane protein, implicated in controlling mitochondrial fission. Upon overexpression of MTP18, mitochondrial morphology was altered from filamentous to punctate structures suggesting excessive mitochondrial fission. Mitochondrial fragmentation was blocked in cells coexpressing either the mitochondrial fusion protein Mfn1 or Drp1[superscript K38A], a dominant negative version of the fission protein Drp1. Also, a loss-of function of endogenous MTP18 by RNA interference (RNAi) resulted in highly fused mitochondria. Moreover, MTP18 appears to be required for mitochondrial fission because it is blocked after overexpression of hFis1 in cells with RNAi-mediated MTP18 knockdown. 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Mitochondrial fission is regulated by a conserved protein complex assembled at the outer membrane. Human MTP18 is a novel nuclear-encoded mitochondrial membrane protein, implicated in controlling mitochondrial fission. Upon overexpression of MTP18, mitochondrial morphology was altered from filamentous to punctate structures suggesting excessive mitochondrial fission. Mitochondrial fragmentation was blocked in cells coexpressing either the mitochondrial fusion protein Mfn1 or Drp1[superscript K38A], a dominant negative version of the fission protein Drp1. Also, a loss-of function of endogenous MTP18 by RNA interference (RNAi) resulted in highly fused mitochondria. Moreover, MTP18 appears to be required for mitochondrial fission because it is blocked after overexpression of hFis1 in cells with RNAi-mediated MTP18 knockdown. In conclusion, we propose that MTP18 functions as an essential intramitochondrial component of the mitochondrial division apparatus, contributing to the maintenance of mitochondrial morphology.</description><subject>Animals</subject><subject>Cells, Cultured</subject><subject>Chlorocebus aethiops</subject><subject>COS Cells</subject><subject>Dynamins</subject><subject>Endopeptidase K</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>GTP Phosphohydrolases - physiology</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Intracellular Membranes - metabolism</subject><subject>Membrane Proteins</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Microtubule-Associated Proteins - physiology</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondria - physiology</subject><subject>Mitochondrial Proteins - antagonists & inhibitors</subject><subject>Mitochondrial Proteins - biosynthesis</subject><subject>Mitochondrial Proteins - genetics</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Mitochondrial Proteins - physiology</subject><subject>RNA Interference</subject><subject>Subcellular Fractions - metabolism</subject><subject>Transfection</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0EtLxDAUBeAgio6jC_-AdiW4qN6b122XMvgCRcFxHTJtopG20aaz8N_bcQbElasLl4_D4TB2hHCOXPKL9yqdA5eottgEJVFeoqBtNgHgmJdKiD22n9I7ABAvaZftoSoLJXU5Yc9tGGL1Fru6D7bJPvo4uNBlD_MnLLIqdkMfFsvBpWyI2V_qQ0ohdtmoW9u2tgm2yyrXNOmA7XjbJHe4uVM2v76az27z-8ebu9nlfV5J0kNekuNQk_AFWSCwqrJCSAJpiTwf3867mlsCIbHWldeilgLRW60LWoCYstN17Fj6c-nSYNqQVgVs5-IyGV0AJ6n0vxBJaSVlMcKzNaz6mFLvvPnoQ2v7L4NgVkubcWnzs_Rojzehy0Xr6l-5mXYEJ2vgbTT2tQ_JvDxzQAEIiBKU-AYfCYJg</recordid><startdate>20050715</startdate><enddate>20050715</enddate><creator>Tondera, Daniel</creator><creator>Czauderna, Frank</creator><creator>Paulick, Katharina</creator><creator>Schwarzer, Rolf</creator><creator>Kaufmann, Jörg</creator><creator>Santel, Ansgar</creator><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20050715</creationdate><title>mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells</title><author>Tondera, Daniel ; Czauderna, Frank ; Paulick, Katharina ; Schwarzer, Rolf ; Kaufmann, Jörg ; Santel, Ansgar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-97e20d73f87a070a5ca334704a77f23f8efed2a70341d6cf63d4311fa6687b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Cells, Cultured</topic><topic>Chlorocebus aethiops</topic><topic>COS Cells</topic><topic>Dynamins</topic><topic>Endopeptidase K</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>GTP Phosphohydrolases - physiology</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Intracellular Membranes - metabolism</topic><topic>Membrane Proteins</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Microtubule-Associated Proteins - physiology</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondria - physiology</topic><topic>Mitochondrial Proteins - antagonists & inhibitors</topic><topic>Mitochondrial Proteins - biosynthesis</topic><topic>Mitochondrial Proteins - genetics</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Mitochondrial Proteins - physiology</topic><topic>RNA Interference</topic><topic>Subcellular Fractions - metabolism</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tondera, Daniel</creatorcontrib><creatorcontrib>Czauderna, Frank</creatorcontrib><creatorcontrib>Paulick, Katharina</creatorcontrib><creatorcontrib>Schwarzer, Rolf</creatorcontrib><creatorcontrib>Kaufmann, Jörg</creatorcontrib><creatorcontrib>Santel, Ansgar</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tondera, Daniel</au><au>Czauderna, Frank</au><au>Paulick, Katharina</au><au>Schwarzer, Rolf</au><au>Kaufmann, Jörg</au><au>Santel, Ansgar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2005-07-15</date><risdate>2005</risdate><volume>118</volume><issue>14</issue><spage>3049</spage><epage>3059</epage><pages>3049-3059</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>Mitochondria are dynamic organelles that change morphology by controlled fission and fusion events. Mitochondrial fission is regulated by a conserved protein complex assembled at the outer membrane. Human MTP18 is a novel nuclear-encoded mitochondrial membrane protein, implicated in controlling mitochondrial fission. Upon overexpression of MTP18, mitochondrial morphology was altered from filamentous to punctate structures suggesting excessive mitochondrial fission. Mitochondrial fragmentation was blocked in cells coexpressing either the mitochondrial fusion protein Mfn1 or Drp1[superscript K38A], a dominant negative version of the fission protein Drp1. Also, a loss-of function of endogenous MTP18 by RNA interference (RNAi) resulted in highly fused mitochondria. Moreover, MTP18 appears to be required for mitochondrial fission because it is blocked after overexpression of hFis1 in cells with RNAi-mediated MTP18 knockdown. In conclusion, we propose that MTP18 functions as an essential intramitochondrial component of the mitochondrial division apparatus, contributing to the maintenance of mitochondrial morphology.</abstract><cop>England</cop><pmid>15985469</pmid><doi>10.1242/jcs.02415</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Company of Biologists |
| subjects | Animals Cells, Cultured Chlorocebus aethiops COS Cells Dynamins Endopeptidase K GTP Phosphohydrolases - metabolism GTP Phosphohydrolases - physiology HeLa Cells Humans Intracellular Membranes - metabolism Membrane Proteins Microtubule-Associated Proteins - metabolism Microtubule-Associated Proteins - physiology Mitochondria - metabolism Mitochondria - physiology Mitochondrial Proteins - antagonists & inhibitors Mitochondrial Proteins - biosynthesis Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Mitochondrial Proteins - physiology RNA Interference Subcellular Fractions - metabolism Transfection |
| title | mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells |
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