Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission

Kurt J. De Vos, Victoria J. Allan, Andrew J. Grierson, Michael P. Sheetz

    Research output: Contribution to journalArticlepeer-review


    Mitochondria display a variety of shapes, ranging from small and spherical or the classical tubular shape to extended networks [1, 2]. Shape transitions occur frequently and include fusion, fission, and branching [3]. It was reported that some mitochondrial shape transitions are developmentally regulated [4, 5], whereas others were linked to disease [6-9] or apoptosis [10, 11]. However, if and how mitochondrial function controls mitochondrial shape through regulation of mitochondrial fission and fusion is unclear. Here, we show that inhibitors of electron transport, ATP synthase, or the permeability transition pore (mtPTP) induced reversible mitochondrial fission. Mitochondrial fission depended on dynamin-related protein 1 (DRP1) and F-actin: Disruption of F-actin attenuated fission and recruitment of DRP1 to mitochondria. In contrast, uncoupling of electron transport and oxidative phosphorylation caused mitochondria to adopt a distinct disk shape. This shape change was independent of the cytoskeleton and DRP1 and was most likely caused by swelling. Thus, disruption of mitochondrial function rapidly and reversibly altered mitochondrial shape either by activation of DRP1-dependent fission or by swelling, indicating a close relationship between mitochondrial fission, shape, and function. Furthermore, our results suggest that the actin cytoskeleton is involved in mitochondrial fission by facilitating mitochondrial recruitment of DRP1. ©2005 Elsevier Ltd All rights reserved.
    Original languageEnglish
    Pages (from-to)678-683
    Number of pages5
    JournalCurrent Biology
    Issue number7
    Publication statusPublished - 12 Apr 2005


    Dive into the research topics of 'Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission'. Together they form a unique fingerprint.

    Cite this