Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion.

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 Lett

journal_title

FEBS letters

authors

Zick M,Duvezin-Caubet S,Schäfer A,Vogel F,Neupert W,Reichert AS

doi

10.1016/j.febslet.2009.05.053

subject

Has Abstract

pub_date

2009-07-07 00:00:00

pages

2237-43

issue

13

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00442-6

journal_volume

583

pub_type

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