AI Article Synopsis
- Loss of VDAC2 in mammalian cells results in problems with the creation of peroxisomes, which are important for cellular metabolism.
- Knockdown of VDAC2 can help restore peroxisome production, changing the location of the protein BAK from mitochondria to peroxisomes.
- The study suggests that BAK plays a key role in controlling the permeability of peroxisomal membranes, especially when BAK activators are overexpressed in normal cells.
Article Abstract
Loss of voltage-dependent anion channel 2 (VDAC2) leads to impaired peroxisome biogenesis in mammalian cells. Knockdown of restores peroxisomal biogenesis in VDAC2-deficient cells, where BAK localization shifts from mitochondria to peroxisomes. Moreover, overexpression of BAK activators in wild-type cells permeabilizes peroxisomes in a BAK-dependent manner. Together, BAK most likely regulates peroxisomal membrane permeability.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5462519 | PMC |
| http://dx.doi.org/10.1080/23723556.2017.1306610 | DOI Listing |
Publication Analysis
Top Keywords
bak regulates
8
bak
4
regulates catalase
4
catalase release
4
release peroxisomes
4
peroxisomes loss
4
loss voltage-dependent
4
voltage-dependent anion
4
anion channel
4
channel vdac2
4
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!