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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2009-7-6
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
7
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pubmed:volume |
583
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2237-43
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pubmed:meshHeading |
pubmed-meshheading:19505460-Dynamins,
pubmed-meshheading:19505460-GTP Phosphohydrolases,
pubmed-meshheading:19505460-GTP-Binding Proteins,
pubmed-meshheading:19505460-Membrane Fusion,
pubmed-meshheading:19505460-Membrane Proteins,
pubmed-meshheading:19505460-Microscopy, Immunoelectron,
pubmed-meshheading:19505460-Mitochondria,
pubmed-meshheading:19505460-Mitochondrial Proteins,
pubmed-meshheading:19505460-Protein Isoforms,
pubmed-meshheading:19505460-Saccharomyces cerevisiae Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion.
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pubmed:affiliation |
Adolf-Butenandt-Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, München, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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