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Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein.

Authors: Jofuku, Akihiro  Ishihara, Naotada  Mihara, Katsuyoshi 
Citation: Jofuku A, etal., Biochem Biophys Res Commun. 2005 Jul 29;333(2):650-9.
Pubmed: (View Article at PubMed) PMID:15979461
DOI: Full-text: DOI:10.1016/j.bbrc.2005.05.154

In yeast, mitochondrial-fission is regulated by the cytosolic dynamin-like GTPase (Dnm1p) in conjunction with a peripheral protein, Mdv1p, and a C-tail-anchored outer membrane protein, Fis1p. In mammals, a dynamin-related protein (Drp1) and Fis1 are involved in the mitochondrial-fission reaction as Dnm1 and Fis1 orthologues, respectively. The involvement of other component(s), such as the Mdv1 homologue, and the mechanisms regulating mitochondrial-fission remain unclear. Here, we identified rat Fis1 (rFis1) and analyzed its structure-function relationship. Blue-native-polyacrylamide gel electrophoresis revealed that rFis1 formed a approximately 200-kDa complex in the outer mitochondrial membrane. Its expression in HeLa cells promoted extensive mitochondrial fragmentation, and gene knock-down by RNAi induced extension of the mitochondrial networks. Taking advantage of these properties, we analyzed functional domains of rFis1. These experiments revealed that the N-terminal and C-terminal segments are both essential for oligomeric rFis1 interaction, and the middle TPR-like domains regulate proper oligomer assembly. Any mutations that disturb the proper oligomeric assembly compromise mitochondrial division-stimulating activity of rFis1.


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CRRD Object Information
CRRD ID: 12738370
Created: 2017-02-01
Species: All species
Last Modified: 2017-02-01
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.