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The 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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Detalles Bibliográficos
Autores principales: Karren, Mary Anne, Coonrod, Emily M., Anderson, Teresa K., Shaw, Janet M.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171191/
https://www.ncbi.nlm.nih.gov/pubmed/16247028
http://dx.doi.org/10.1083/jcb.200506158
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author Karren, Mary Anne
Coonrod, Emily M.
Anderson, Teresa K.
Shaw, Janet M.
author_facet Karren, Mary Anne
Coonrod, Emily M.
Anderson, Teresa K.
Shaw, Janet M.
author_sort Karren, Mary Anne
collection PubMed
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 NH(2)-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 NH(2)-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.
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spelling pubmed-21711912008-03-05 The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly Karren, Mary Anne Coonrod, Emily M. Anderson, Teresa K. Shaw, Janet M. J Cell Biol Research Articles 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 NH(2)-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 NH(2)-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. The Rockefeller University Press 2005-10-24 /pmc/articles/PMC2171191/ /pubmed/16247028 http://dx.doi.org/10.1083/jcb.200506158 Text en Copyright © 2005, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Karren, Mary Anne
Coonrod, Emily M.
Anderson, Teresa K.
Shaw, Janet M.
The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
title The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
title_full The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
title_fullStr The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
title_full_unstemmed The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
title_short The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
title_sort role of fis1p–mdv1p interactions in mitochondrial fission complex assembly
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171191/
https://www.ncbi.nlm.nih.gov/pubmed/16247028
http://dx.doi.org/10.1083/jcb.200506158
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