Langer, A., Wilson, J.R., Howard, L. et al. Sci Rep 16, 3,488 (2026). https://doi.org/10.1038/s41598-025-27476-x.
Get the latest international news and world events from around the world.
Neuron position found less crucial for brain connectivity than once thought
The human brain contains billions of connected neurons that collectively support different mental functions, including the processing of sensory information, the encoding of memories, attention processes, and decision-making. For a long time, neuroscientists have assumed the position of specific neurons in the brain plays a key role in the brain’s connectivity and proper functioning.
Researchers at University of Geneva, INSERM, Ecole Polytechnique Fédérale de Lausanne and other institutes recently gathered evidence that contradicts this long-standing assumption, showing misplaced neurons can still retain their “identity,” connect with other neurons and support the processing of sensory information.
Their paper, published in Nature Neuroscience, could reshape the present understanding of developmental disorders and other conditions linked to the rearrangement of neurons or cortical malformations.
Different Autism Mutations Can Lead to Similar Brain Changes
The shared pathways were linked to neuron maturation, synapse formation, and the control of gene activity. Further analysis pointed to a group of genes involved in organizing DNA and regulating which genes are switched on or off. These genes sit high in the regulatory chain, influencing many downstream processes previously linked to autism.
To test whether this network played an active role, the team reduced the activity of several key regulators using CRISPR-based methods in neural cells. This led to downstream changes similar to those seen in the autism models.
However, organoids from individuals with idiopathic autism showed less consistent changes, likely reflecting the complex and distributed genetic risk seen in most autism cases.
CLN3 mediates chloride efflux from lysosomes
Lysosomes degrade damaged organelles and macromolecules to recycle nutrient components. Lysosomal storage diseases (LSDs) are linked to mutations of genes encoding lysosomal proteins and may lead to age-related disorders, including neurodegenerative diseases. But, how lysosomal dysfunction contributes to neurodegenerative diseases is not clear yet…
The researchers identify CLN3 (ceroid lipofuscinosis, neuronal 3), linked to Batten disease as a conserved lysosomal protein that regulates lysosomal chloride homeostasis, pH, and protein degradation.
Curcumin analog C1 is a natural compound with anti-inflammatory properties could enhance CLN3 activity and improve lysosomal function by activating TFEB. sciencenewshighlights ScienceMission https://sciencemission.com/CLN3-n-chloride-efflux-n-lysosomes
Wang et al. identify CLN3 as a conserved lysosomal protein that regulates lysosomal chloride homeostasis, pH, and protein degradation. Transcription factor EB (TFEB) activation enhances CLN3 function, revealing the TFEB-CLN3 signaling axis as a promising therapeutic target for lysosomal storage disorders.