role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly
Mitochondrial division requires coordinated interactions among Fis1p, Mdv1p, and the Dnm1p GTPase, which assemble into fission complexes on the outer mitochondrial membrane. The integral outer membrane protein Fis1p contains a cytoplasmic domain consisting of a tetratricopeptide repeat (TPR)-like fo...
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| Veröffentlicht in: | The Journal of cell biology 2005-10, Vol.171 (2), p.291-301 |
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| container_title | The Journal of cell biology |
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| creator | Karren, Mary Anne Coonrod, Emily M Anderson, Teresa K Shaw, Janet M |
| description | Mitochondrial division requires coordinated interactions among Fis1p, Mdv1p, and the Dnm1p GTPase, which assemble into fission complexes on the outer mitochondrial membrane. The integral outer membrane protein Fis1p contains a cytoplasmic domain consisting of a tetratricopeptide repeat (TPR)-like fold and a short NH₂-terminal helix. Although it is known that the cytoplasmic domain is necessary for assembly of Mdv1p and Dnm1p into fission complexes, the molecular details of this assembly are not clear. In this study, we provide new evidence that the Fis1p-Mdv1p interaction is direct. Furthermore, we show that conditional mutations in the Fis1p TPR-like domain cause fission complex assembly defects that are suppressed by mutations in the Mdv1p-predicted coiled coil. We also define separable functions for the Fis1p NH₂-terminal arm and TPR-like fold. These studies suggest that the concave binding surface of the Fis1p TPR-like fold interacts with Mdv1p during mitochondrial fission and that Mdv1p facilitates Dnm1p recruitment into functional fission complexes. |
| doi_str_mv | 10.1083/jcb.200506158 |
| format | Article |
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The integral outer membrane protein Fis1p contains a cytoplasmic domain consisting of a tetratricopeptide repeat (TPR)-like fold and a short NH₂-terminal helix. Although it is known that the cytoplasmic domain is necessary for assembly of Mdv1p and Dnm1p into fission complexes, the molecular details of this assembly are not clear. In this study, we provide new evidence that the Fis1p-Mdv1p interaction is direct. Furthermore, we show that conditional mutations in the Fis1p TPR-like domain cause fission complex assembly defects that are suppressed by mutations in the Mdv1p-predicted coiled coil. We also define separable functions for the Fis1p NH₂-terminal arm and TPR-like fold. These studies suggest that the concave binding surface of the Fis1p TPR-like fold interacts with Mdv1p during mitochondrial fission and that Mdv1p facilitates Dnm1p recruitment into functional fission complexes.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200506158</identifier><identifier>PMID: 16247028</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adaptor Proteins, Signal Transducing ; Alleles ; Antibodies ; Apoptosis ; Carrier Proteins - metabolism ; Cell division ; Cell growth ; Genetic mutation ; GTP Phosphohydrolases - metabolism ; Membranes ; Mitochondria ; Mitochondria - metabolism ; Mitochondrial DNA ; Mitochondrial Proteins - metabolism ; Mutation ; Phenotypes ; Plasmids ; Polymerase chain reaction ; Protein Conformation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; Temperature ; Yeasts</subject><ispartof>The Journal of cell biology, 2005-10, Vol.171 (2), p.291-301</ispartof><rights>Copyright 2005 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Oct 24, 2005</rights><rights>Copyright © 2005, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-fd9a5e3cc0c72700a5b8568f1e86f43619ee588336adaf6bfcad1607c3b8a2883</citedby><cites>FETCH-LOGICAL-c554t-fd9a5e3cc0c72700a5b8568f1e86f43619ee588336adaf6bfcad1607c3b8a2883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16247028$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karren, Mary Anne</creatorcontrib><creatorcontrib>Coonrod, Emily M</creatorcontrib><creatorcontrib>Anderson, Teresa K</creatorcontrib><creatorcontrib>Shaw, Janet M</creatorcontrib><title>role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Mitochondrial division requires coordinated interactions among Fis1p, Mdv1p, and the Dnm1p GTPase, which assemble into fission complexes on the outer mitochondrial membrane. The integral outer membrane protein Fis1p contains a cytoplasmic domain consisting of a tetratricopeptide repeat (TPR)-like fold and a short NH₂-terminal helix. Although it is known that the cytoplasmic domain is necessary for assembly of Mdv1p and Dnm1p into fission complexes, the molecular details of this assembly are not clear. In this study, we provide new evidence that the Fis1p-Mdv1p interaction is direct. Furthermore, we show that conditional mutations in the Fis1p TPR-like domain cause fission complex assembly defects that are suppressed by mutations in the Mdv1p-predicted coiled coil. We also define separable functions for the Fis1p NH₂-terminal arm and TPR-like fold. These studies suggest that the concave binding surface of the Fis1p TPR-like fold interacts with Mdv1p during mitochondrial fission and that Mdv1p facilitates Dnm1p recruitment into functional fission complexes.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Alleles</subject><subject>Antibodies</subject><subject>Apoptosis</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell division</subject><subject>Cell growth</subject><subject>Genetic mutation</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>Membranes</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial DNA</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Mutation</subject><subject>Phenotypes</subject><subject>Plasmids</subject><subject>Polymerase chain reaction</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Temperature</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAURi0EokNhyQ5BxKK7lHvt-JENEqraQlXEArq2HMduPUriYGeq9t_jMqPhsenKss7R53v9EfIa4RhBsQ9r2x1TAA4CuXpCVsgbqBU28JSsACjWLaf8gLzIeQ0AjWzYc3KAgjYSqFqRixQHV0VfnYWMc_21v8W5CtPikrFLiFMul2oMS7Q3cepTMEPlQ86FVDaO8-DuKpOzG7vh_iV55s2Q3avdeUiuzk5_nHyuL7-dfzn5dFlbzpul9n1ruGPWgpVUAhjeKS6UR6eEb5jA1jmuFGPC9MaLzlvTowBpWacMLeCQfNzmzptudL1105LMoOcURpPudTRB_0umcKOv462mKBFbLAFHu4AUf25cXvQYsnXDYCYXN1kLJWmjUDwqomSq5S0r4vv_xHXcpKn8wu9HAVrJi1RvJZtizsn5_cgI-qFLXbrU-y6L__bvPf_Yu_KK8GYrrPMS054zwVUDD9O_22JvojbXKWR99Z0CMkBgQkpkvwDBE61C</recordid><startdate>20051024</startdate><enddate>20051024</enddate><creator>Karren, Mary Anne</creator><creator>Coonrod, Emily M</creator><creator>Anderson, Teresa K</creator><creator>Shaw, Janet M</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20051024</creationdate><title>role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly</title><author>Karren, Mary Anne ; Coonrod, Emily M ; Anderson, Teresa K ; Shaw, Janet M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c554t-fd9a5e3cc0c72700a5b8568f1e86f43619ee588336adaf6bfcad1607c3b8a2883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Alleles</topic><topic>Antibodies</topic><topic>Apoptosis</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell division</topic><topic>Cell growth</topic><topic>Genetic mutation</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>Membranes</topic><topic>Mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial DNA</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Mutation</topic><topic>Phenotypes</topic><topic>Plasmids</topic><topic>Polymerase chain reaction</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Temperature</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karren, Mary Anne</creatorcontrib><creatorcontrib>Coonrod, Emily M</creatorcontrib><creatorcontrib>Anderson, Teresa K</creatorcontrib><creatorcontrib>Shaw, Janet M</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karren, Mary Anne</au><au>Coonrod, Emily M</au><au>Anderson, Teresa K</au><au>Shaw, Janet M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2005-10-24</date><risdate>2005</risdate><volume>171</volume><issue>2</issue><spage>291</spage><epage>301</epage><pages>291-301</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Mitochondrial division requires coordinated interactions among Fis1p, Mdv1p, and the Dnm1p GTPase, which assemble into fission complexes on the outer mitochondrial membrane. The integral outer membrane protein Fis1p contains a cytoplasmic domain consisting of a tetratricopeptide repeat (TPR)-like fold and a short NH₂-terminal helix. Although it is known that the cytoplasmic domain is necessary for assembly of Mdv1p and Dnm1p into fission complexes, the molecular details of this assembly are not clear. In this study, we provide new evidence that the Fis1p-Mdv1p interaction is direct. Furthermore, we show that conditional mutations in the Fis1p TPR-like domain cause fission complex assembly defects that are suppressed by mutations in the Mdv1p-predicted coiled coil. We also define separable functions for the Fis1p NH₂-terminal arm and TPR-like fold. These studies suggest that the concave binding surface of the Fis1p TPR-like fold interacts with Mdv1p during mitochondrial fission and that Mdv1p facilitates Dnm1p recruitment into functional fission complexes.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>16247028</pmid><doi>10.1083/jcb.200506158</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Alleles Antibodies Apoptosis Carrier Proteins - metabolism Cell division Cell growth Genetic mutation GTP Phosphohydrolases - metabolism Membranes Mitochondria Mitochondria - metabolism Mitochondrial DNA Mitochondrial Proteins - metabolism Mutation Phenotypes Plasmids Polymerase chain reaction Protein Conformation Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Temperature Yeasts |
| title | role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly |
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