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First published online November 27, 2006

Journal of Cell Science 119, 2305e (2006)
© The Company of Biologists Limited
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In this issue

Make or break time for mitochondria


Figure 1

Mitochondria are dynamic structures, constantly undergoing fusion and fission. These two processes play important roles in cellular physiology and cell death, and key components of their machinery have been identified. However, what regulates the balance between fusion and fission is unclear. Katsuyoshi Mihara and colleagues now identify a mammalian protein - mitofusin-binding protein (MIB) - that regulates mitochondrial fusion by interacting with mitofusins (Mfns), mitochondrial outer-membrane GTPases that are required for mitochondrial fusion (see p. 4913). The authors isolated MIB, which binds to mitochondrial membranes, from rat cytosol by using affinity purification with recombinant Mfn. Overexpression of MIB, they report, induces mitochondrial fragmentation in HeLa cells, whereas knocking it down by RNAi induces an expansion of mitochondrial network structures and inhibits cell growth. Knocking down both MIB and Mfn1, however, causes mitochondrial fragmentation, which indicates that MIB functions as a negative regulator of Mfn1-dependent mitochondrial fusion. The authors therefore conclude that MIB plays an essential role in cellular function by regulating mitochondrial dynamics in cooperation with Mfn proteins.


Related articles in JCS:

Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function
Yuka Eura, Naotada Ishihara, Toshihiko Oka, and Katsuyoshi Mihara
JCS 2006 119: 4913-4925. [Abstract] [Full Text]  




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