Regulation of endoplasmic reticulum-mitochondria transfer and its importance in GBM

Jinyi Zhao1,2, Tian Li3,4, Yue Jing3,4

  • 1School of Medicine, Huanghuai University, Zhumadian, China.

PubMed

Insights

Mitochondria and endoplasmic reticulum connections, known as MAM, are vital for cell health. Their dysfunction is linked to glioblastoma, highlighting MAM

Area of Science:

  • Cell Biology
  • Organelle Biology
  • Cancer Research

Background:

  • Organelles were traditionally viewed as isolated units.
  • Emerging evidence highlights dynamic inter-organelle connections.
  • Mitochondrial-associated endoplasmic reticulum membrane (MAM) is a key contact site.

Purpose of the Study:

  • To review the role and mechanisms of MAM.
  • To explore the link between MAM dysfunction and glioblastoma.

Main Methods:

  • Literature review of studies on MAM.
  • Analysis of research on ER-mitochondria interactions.
  • Synthesis of data on glioblastoma and MAM.

Main Results:

  • MAM regulates lipid metabolism, calcium homeostasis, and apoptosis.
  • MAM is a critical hub for intracellular signaling.
  • Evidence links MAM dysfunction to tumorigenesis, especially glioblastoma.

Conclusions:

  • MAM plays a crucial role in maintaining cellular homeostasis.
  • Dysregulation of the ER-mitochondria axis is implicated in glioblastoma development.
  • Further research into MAM mechanisms is warranted for therapeutic strategies.

Related Concept Videos

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,...
12.1K
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
21.0K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.0K
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
7.8K
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
4.7K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
16.5K