Related Experiment Video

Updated: Aug 8, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane

A M Labrousse1, M D Zappaterra, D A Rube

  • 1Department of Biological Chemistry, University of California, Los Angeles School of Medicine 90095, USA.

Molecular Cell
|January 5, 2000
PubMed

Insights

Mitochondrial division is clarified: mutations in dynamin-related protein 1 (DRP-1) disrupt outer membrane scission. Overexpressed DRP-1 causes fragmentation, revealing its role in mitochondrial outer membrane division.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The precise mechanisms governing mitochondrial division remain largely uncharacterized.
  • Mitochondrial dynamics, including division and fusion, are crucial for cellular function and health.

Purpose of the Study:

  • To investigate the role of dynamin-related protein 1 (DRP-1) in the process of mitochondrial division.
  • To elucidate the specific stage of mitochondrial division regulated by DRP-1.

Main Methods:

  • Utilized genetic mutations in C. elegans to study DRP-1 function in mitochondria.
  • Employed overexpression of wild-type DRP-1 and DRP-1 fused to GFP to observe mitochondrial morphology.
  • Analyzed mitochondrial membrane integrity and fragmentation patterns.

Main Results:

  • Mutations in DRP-1 led to the retraction of the mitochondrial matrix, with outer membrane tubules surrounding blebs, indicating inhibited outer membrane scission.
  • Inner membrane scission still occurred in mutant DRP-1.
  • Overexpression of wild-type DRP-1 resulted in excessive mitochondrial fragmentation, suggesting an active role in scission.
  • DRP-1 fused to GFP localized to sites of mitochondrial scission.

Conclusions:

  • DRP-1 plays a critical role in the final stages of mitochondrial division.
  • DRP-1 specifically regulates the scission of the mitochondrial outer membrane.
  • These findings provide key insights into the molecular machinery of mitochondrial division.

More Related Videos

Studying Mitochondrial Structure and Function in Drosophila Ovaries09:53

Studying Mitochondrial Structure and Function in Drosophila Ovaries

Published on: January 4, 2017

Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans08:47

Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans

Published on: July 5, 2019

Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...