The mitochondrial dynamin-like GTPase Mgm1 exists as a long (l-Mgm1) and a short isoform (s-Mgm1). They both are essential for mitochondrial fusion. Here we show that the isoforms interact in a homotypic and heterotypic manner. Their submitochondrial distribution between inner boundary membrane and cristae was markedly different. Overexpression of l-Mgm1 exerts a dominant negative effect on mitochondrial fusion. A functional GTPase domain is required only in s-Mgm1 but not in l-Mgm1. We propose that l-Mgm1 acts primarily as an anchor in the inner membrane that in concert with the GTPase activity of s-Mgm1 mediates the fusion of inner membranes.
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| rdf:type | |
| rdfs:comment |
The mitochondrial dynamin-like GTPase Mgm1 exists as a long (l-Mgm1) and a short isoform (s-Mgm1). They both are essential for mitochondrial fusion. Here we show that the isoforms interact in a homotypic and heterotypic manner. Their submitochondrial distribution between inner boundary membrane and cristae was markedly different. Overexpression of l-Mgm1 exerts a dominant negative effect on mitochondrial fusion. A functional GTPase domain is required only in s-Mgm1 but not in l-Mgm1. We propose that l-Mgm1 acts primarily as an anchor in the inner membrane that in concert with the GTPase activity of s-Mgm1 mediates the fusion of inner membranes.
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| uniprot:name |
FEBS Lett.
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| uniprot:author |
Duvezin-Caubet S.,
Neupert W.,
Reichert A.S.,
Schafer A.,
Vogel F.,
Zick M.
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| uniprot:date |
2009
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| uniprot:pages |
2237-2243
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| uniprot:title |
Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion.
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| uniprot:volume |
583
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| dc-term:identifier |
doi:10.1016/j.febslet.2009.05.053
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