Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zick M,Duvezin-Caubet S,Schäfer A,Vogel F,Neupert W,Reichert ASdoi
10.1016/j.febslet.2009.05.053subject
Has Abstractpub_date
2009-07-07 00:00:00pages
2237-43issue
13eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00442-6journal_volume
583pub_type
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