Mitochondrial Fission: A Non-Nuclear Role for Num1p

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Mitochondrial Fission: A Non-Nuclear Role for Num1p Astrid C. Schauss, Heidi M. McBride  Current Biology  Volume 17, Issue 12, Pages R467-R470 (June 2007) DOI: 10.1016/j.cub.2007.04.018 Copyright © 2007 Elsevier Ltd Terms and Conditions

Figure 1 Model for the role of Num1p in mitochondrial segregation and fission. (A) Retrograde mitochondrial movement (mitochondria shown in grey) results from the insertion of new actin monomers into the barbed end of the growing filament within the bud tip (shown as lighter blue). This actin polymerization is mediated by the formin Bni1p, which also recruits Num1p to the pole. We speculate that during mitosis the Bni1p–Num1p complex may function to anchor mitochondria through the interactions between Num1p and the dynamin-related GTPase Dnm1p, as shown by Jensen and colleagues [1]. Once the mitochondria fragment, they would then become anchored to the growing actin cable through the actin-binding mitochore complex and travel back towards the mother cell. Anterograde movement of mitochondria into the bud tip has been shown to be mediated by actin polymerization from the mitochondrial-associated Arp2/3 complex. This complex requires Jsn1p for mitochondrial membrane association. Num1p and Bni1p complexes, although enriched at the daughter pole during mitosis, are not exclusive to the bud tip. Their peripheral localizations probably help to facilitate mitochondrial fission events throughout the cell. The two boxed regions represent potential fission events that are expanded upon in (B). (B) The activation of Rho GTPases at the cell surface leads to the recruitment of Bni1p, which regulates the formation of actin cables. Bni1p recruits Num1p to these sites, thereby placing Num1p at active sites of cytoskeletal assembly. Jensen and colleagues [1] have shown that Num1p anchors mitochondria to the plasma membrane through its interaction with PI(4,5)P2 and Dnm1p. This cortically anchored Dnm1p may bind to the integral membrane protein Fis1p via the adaptor proteins Mdv1p or Caf4p. At sites of fission, Dnm1p forms spirals that constrict in a GTP-dependent manner. If the mitochore complex anchors one half of the dividing mitochondrion, then the force of the growing actin cable may provide the required tension within the constricted region that aids the process of membrane scission. Current Biology 2007 17, R467-R470DOI: (10.1016/j.cub.2007.04.018) Copyright © 2007 Elsevier Ltd Terms and Conditions