Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Mitochondrial shaping cuts.

Mafalda Escobar-Henriques1, Thomas Langer

  • 1Institute of Genetics and Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany. Mafalda.Escobar@uni-koeln.de

Biochimica Et Biophysica Acta
|May 27, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Vitamin C appears harmful in patients after out-of-hospital cardiac arrest treated in the intensive care unit.

Intensive care medicine·2026
Same author

Limiting neurodegeneration in ALS: A phosphatase paves the way.

Neuron·2026
Same author

Mitochondria limit coenzyme Q export under cholesterol biosynthetic stress.

The Journal of cell biology·2026
Same author

Regional citrate anticoagulation for renal replacement therapy during venovenous ECMO: A randomized crossover pilot study.

Annals of intensive care·2026
Same author

MTCH2 promotes BAX and BAK self-assembly and apoptotic pore growth.

Nature structural & molecular biology·2026
Same author

Proteolytic control of mitochondrial protein translocases.

Protein science : a publication of the Protein Society·2026
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Proteolysis regulates mitochondrial morphology by controlling fusion and fission. Key proteins like GTPase Fzo1 and GTPase Mgm1 are degraded or processed, impacting mitochondrial dynamics.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Proteolytic events are crucial for regulating diverse cellular processes.
  • Mitochondrial morphology is dynamically regulated by fusion and fission events.
  • The core machinery governing mitochondrial fusion is subject to proteolytic control.

Purpose of the Study:

  • To review the regulatory roles of proteolysis in mitochondrial plasticity.
  • To summarize the current understanding of how proteolysis impacts mitochondrial dynamics.

Main Methods:

  • Literature review of studies on proteolysis and mitochondrial dynamics.
  • Analysis of proteolytic pathways affecting mitochondrial fusion components.

Main Results:

Related Experiment Videos

  • Two key components of mitochondrial fusion machinery are under proteolytic control.
  • GTPase Fzo1 undergoes degradation via two independent proteolytic pathways.
  • GTPase Mgm1 processing by rhomboid protease Pcp1 is essential for fusion.

Conclusions:

  • Proteolysis plays a significant regulatory role in mitochondrial morphology and plasticity.
  • Emerging evidence highlights functional links between AAA proteases and mitochondrial dynamics.