Related Experiment Video

Updated: Jun 29, 2025

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

8.9K

GTPBP8 modulates mitochondrial fission through a Drp1-dependent process

Xiumei He1,2,3, Liang Wang2, Hoi Ying Tsang4

  • 1School of Life Sciences, Guangxi Normal University, Guilin 541004, China.

Journal of Cell Science
|April 8, 2024
PubMed

Insights

GTPBP8 is crucial for mitochondrial fission in mammalian cells. Its regulation impacts oxidative stress and the recruitment of Drp1, a key protein in mitochondrial division.

Area of Science:

  • Cell Biology
  • Mitochondrial Dynamics
  • Molecular Mechanisms

Background:

  • Mitochondrial fission is essential for cellular health, involving complex protein interactions and signaling pathways.
  • Regulatory mechanisms governing mitochondrial fission are not fully understood, despite research on fission factors.

Purpose of the Study:

  • To elucidate the role of the mitochondrial GTPase, GTPBP8, in regulating mitochondrial fission in mammalian cells.
  • To investigate the relationship between GTPBP8, oxidative stress, and the mitochondrial fission protein Drp1 (DNM1L).

Main Methods:

  • Depletion and overexpression of GTPBP8 in mammalian cells.
  • Analysis of mitochondrial morphology using microscopy.
  • Assessment of Drp1 (DNM1L) protein levels, phosphorylation, and mitochondrial recruitment.

Main Results:

  • GTPBP8 depletion caused mitochondrial elongation; GTPBP8 overexpression induced mitochondrial fragmentation.
  • GTPBP8's effect on fragmentation was dependent on the mitochondrial fission protein Drp1 (DNM1L).
  • GTPBP8 downregulation increased oxidative stress and Drp1 (DNM1L) phosphorylation at Ser637, impairing Drp1 recruitment.

Conclusions:

  • GTPBP8 is a critical regulator of mitochondrial fission, influencing the mitochondrial division apparatus.
  • GTPBP8 modulates mitochondrial morphology by affecting Drp1 (DNM1L) recruitment and function.
  • The study highlights GTPBP8's role in maintaining mitochondrial integrity and responding to oxidative stress.
Keywords:
Drp1FissionGTPBP8MitochondriaPhosphorylation

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

24.0K
A Faster, High Resolution, mtPA-GFP-based Mitochondrial Fusion Assay Acquiring Kinetic Data of Multiple Cells in Parallel Using Confocal Microscopy10:45

A Faster, High Resolution, mtPA-GFP-based Mitochondrial Fusion Assay Acquiring Kinetic Data of Multiple Cells in Parallel Using Confocal Microscopy

Published on: July 20, 2012

16.6K

Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
8.3K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.1K
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...
2.1K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
3.5K
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
6.5K
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
2.6K