Related Experiment Video
Updated: Nov 1, 2025

Author Spotlight: Detection of Mitophagy in Caenorhabditis elegans and Mammalian Cells Using Organelle-Specific Dyes
Published on: May 19, 2023
Vacuolar transporter Mnr2 safeguards organellar integrity in aged cells
Md Hashim Reza1,2, Rajesh Patkar2,3, Kaustuv Sanyal1
1Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bengaluru, India.
Abstract:
Aging is associated with altered mitochondrial function, which is dependent on the magnesium (Mg+2 ) ion flux. The molecular mechanism underlying Mg+2 homeostasis, especially during aging has not been well understood. We previously demonstrated that the absence of a vacuolar ion transporter Mnr2 accelerates cell death in the older part of the colony in Magnaporthe oryzae presumably due to an altered Mg+2 homeostasis. Here, we show the localization of Mnr2 as dynamic puncta at the vacuolar membrane, especially in the older Magnaporthe cells. Such vacuolar Mnr2 puncta are often localized in close proximity with the filamentous mitochondria in the older cells. Further, we show loss of integrity of mitochondria and vacuoles in older mnr2∆ null cells. Remarkably, exogenously added Mg+2 restores the mitochondrial structure as well as improves the lifespan of mnr2∆ null cells. Taken together, we propose an ion transporter Mnr2-based Mg+2 homeostasis as a means in preserving mitochondrial and vacuolar integrity and function in older M. oryzae cells.
Insights
Magnesium (Mg+2) ion homeostasis, regulated by the Mnr2 transporter, is crucial for maintaining mitochondrial and vacuolar integrity during aging in Magnaporthe oryzae. Supplementing Mg+2 improves cell lifespan and mitochondrial structure in aging cells.
Area of Science:
- Cell Biology
- Mycology
- Aging Research
Background:
- Aging is linked to impaired mitochondrial function, influenced by magnesium (Mg+2) ion flux.
- The molecular basis of Mg+2 homeostasis during aging remains unclear.
- Previous work showed Mnr2 transporter absence accelerates aging-related cell death in Magnaporthe oryzae.
Purpose of the Study:
- To investigate the role of the Mnr2 transporter in Mg+2 homeostasis during aging in Magnaporthe oryzae.
- To elucidate the relationship between Mnr2, Mg+2, and the integrity of mitochondria and vacuoles in aging fungal cells.
Main Methods:
- Localization studies of the Mnr2 transporter in aging Magnaporthe oryzae cells.
- Microscopy to assess mitochondrial and vacuolar integrity in wild-type and mnr2∆ null cells.
- Experimental manipulation of extracellular Mg+2 levels.
Main Results:
- Mnr2 localizes to dynamic puncta at the vacuolar membrane in older Magnaporthe cells, often near mitochondria.
- Loss of Mnr2 leads to mitochondrial and vacuolar integrity loss in aging cells.
- Exogenous Mg+2 supplementation rescues mitochondrial structure and extends lifespan in mnr2∆ null cells.
Conclusions:
- The Mnr2 transporter plays a key role in maintaining Mg+2 homeostasis in aging Magnaporthe oryzae.
- Mnr2-dependent Mg+2 homeostasis is essential for preserving mitochondrial and vacuolar integrity and function.
- Targeting Mg+2 transport may offer strategies to mitigate aging-related cellular decline.
Related Concept Videos
Export of Misfolded Proteins out of the ER
Nuclear Export of mRNA
Membrane Asymmetry Regulating Transporters
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Receptor Downregulation in MVBs
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
Short-distance Transport of Resources
Overview of Secretory Vesicles
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...

