scholarly journals Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1

2005 ◽  
Vol 118 (18) ◽  
pp. 4141-4151 ◽  
Author(s):  
T. Yu
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Mitochondrial Fission ◽  
Mitochondrial Outer Membrane

scholarly journals Mutations in Fis1 disrupt orderly disposal of defective mitochondria

2014 ◽  
Vol 25 (1) ◽  
pp. 145-159 ◽  
Author(s):  
Qinfang Shen ◽  
Koji Yamano ◽  
Brian P. Head ◽  
Sumihiro Kawajiri ◽  
Jesmine T. M. Cheung ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Couple Stress ◽  
Mitochondrial Fission ◽  
Mitochondrial Outer Membrane ◽  
Related Protein ◽  
Degradation Processes ◽  
Mitochondrial Toxins

Mitochondrial fission is mediated by the dynamin-related protein Drp1 in metazoans. Drp1 is recruited from the cytosol to mitochondria by the mitochondrial outer membrane protein Mff. A second mitochondrial outer membrane protein, named Fis1, was previously proposed as recruitment factor, but Fis1−/− cells have mild or no mitochondrial fission defects. Here we show that Fis1 is nevertheless part of the mitochondrial fission complex in metazoan cells. During the fission cycle, Drp1 first binds to Mff on the surface of mitochondria, followed by entry into a complex that includes Fis1 and endoplasmic reticulum (ER) proteins at the ER–mitochondrial interface. Mutations in Fis1 do not normally affect fission, but they can disrupt downstream degradation events when specific mitochondrial toxins are used to induce fission. The disruptions caused by mutations in Fis1 lead to an accumulation of large LC3 aggregates. We conclude that Fis1 can act in sequence with Mff at the ER–mitochondrial interface to couple stress-induced mitochondrial fission with downstream degradation processes.

scholarly journals MTFR2 regulates mitochondrial fission and impacts spindle integrity during mitosis

2020 ◽  
Author(s):  
Yibo Luo ◽  
Song-Tao Liu
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Chromosome Segregation ◽  
Outer Membrane Protein ◽  
Mitochondrial Fission ◽  
Critical Role ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Fragmentation ◽  
Daughter Cells ◽  
Multipolar Spindles

AbstractPreviously we reported that mitochondrial fission regulator 2 (MTFR2, also termed DUFD1 or FAM54A) is co-transcribed with core centromere/kinetochore components, indicating a possible role in mitosis regulation. Here we show that human MTFR2 is a mitochondrial outer membrane protein and participates in DRP1 dependent mitochondrial fission. Multiple MTFR2 variants identified in cancer samples are defective in triggering mitochondrial fission. Inducible MTFR2 depletion caused prolonged mitotic duration and increased chromosome mis-segregation, resulting in multi-nucleated daughter cells. MTFR2 knockout cells accumulated spindle defects, producing either multipolar spindles or short oscillating spindles due to loss of astral microtubules. MTFR2 is phosphorylated during mitosis. The phosphorylation mutant, as well as the cancer variants, failed to correct the prolonged mitotic duration. MTFR2 knockout also rendered cells more resistant to apoptosis caused by taxol treatment. As overexpressing MFN1 or DRP1-K38A also caused spindle defects, we conclude that mitochondrial fragmentation during mitosis ensures spindle integrity and chromosomal stability, and MTFR2 plays a critical role in bridging proper mitochondrial fission and chromosome segregation.

scholarly journals Multispan mitochondrial outer membrane protein Ugo1 follows a unique Mim1-dependent import pathway

2011 ◽  
Vol 194 (3) ◽  
pp. 397-405 ◽  
Author(s):  
Dražen Papić ◽  
Katrin Krumpe ◽  
Jovana Dukanovic ◽  
Kai S. Dimmer ◽  
Doron Rapaport
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Gel Electrophoresis ◽  
Mitochondrial Outer Membrane ◽  
Yeast Mitochondria ◽  
Membrane Complex ◽  
Native Gel ◽  
Insertion Process ◽  
Import Receptor

The mitochondrial outer membrane (MOM) harbors several multispan proteins that execute various functions. Despite their importance, the mechanisms by which these proteins are recognized and inserted into the outer membrane remain largely unclear. In this paper, we address this issue using yeast mitochondria and the multispan protein Ugo1. Using a specific insertion assay and analysis by native gel electrophoresis, we show that the import receptor Tom70, but not its partner Tom20, is involved in the initial recognition of the Ugo1 precursor. Surprisingly, the import pore formed by the translocase of the outer membrane complex appears not to be required for the insertion process. Conversely, the multifunctional outer membrane protein mitochondrial import 1 (Mim1) plays a central role in mediating the insertion of Ugo1. Collectively, these results suggest that Ugo1 is inserted into the MOM by a novel pathway in which Tom70 and Mim1 contribute to the efficiency and selectivity of the process.

scholarly journals Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET

2017 ◽  
Vol 102 ◽  
pp. 240-247 ◽  
Author(s):  
Aaron P. Landry ◽  
Yiming Wang ◽  
Zishuo Cheng ◽  
Robert B. Crochet ◽  
Yong-Hwan Lee ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Mitochondrial Outer Membrane ◽  
Electron Shuttles

scholarly journals A Novel Isoform of the Mitochondrial Outer Membrane Protein VDAC3 via Alternative Splicing of a 3-Base Exon

1998 ◽  
Vol 273 (46) ◽  
pp. 30482-30486 ◽  
Author(s):  
Margaret J. Sampson ◽  
Lyle Ross ◽  
William K. Decker ◽  
William J. Craigen
Keyword(s):  
Alternative Splicing ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Mitochondrial Outer Membrane
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