Biljana Ermanoska
@biljanaermanoska.bsky.social
Science enthusiast, currently MSCA postdoctoral fellow at UAntwerp. Actin' and forces in synapses.
Reposted by Biljana Ermanoska
My first thought when reading the title was integrins, and it was nice to see that authors established that link bringing together previous and new stuff.
July 13, 2025 at 11:09 AM
My first thought when reading the title was integrins, and it was nice to see that authors established that link bringing together previous and new stuff.
5/5
Together, our findings reveal a mechanically sensitive actin–NMII–integrin system at the NMJ—capable of adapting to tension changes to preserve synaptic structure and function.
Together, our findings reveal a mechanically sensitive actin–NMII–integrin system at the NMJ—capable of adapting to tension changes to preserve synaptic structure and function.
July 12, 2025 at 9:00 PM
5/5
Together, our findings reveal a mechanically sensitive actin–NMII–integrin system at the NMJ—capable of adapting to tension changes to preserve synaptic structure and function.
Together, our findings reveal a mechanically sensitive actin–NMII–integrin system at the NMJ—capable of adapting to tension changes to preserve synaptic structure and function.
4/5
To probe mechanical sensitivity, we used axon severing and stretching. We found that presynaptic actomyosin and integrin organization respond dynamically to loss and gain of tension.
To probe mechanical sensitivity, we used axon severing and stretching. We found that presynaptic actomyosin and integrin organization respond dynamically to loss and gain of tension.
July 12, 2025 at 9:00 PM
4/5
To probe mechanical sensitivity, we used axon severing and stretching. We found that presynaptic actomyosin and integrin organization respond dynamically to loss and gain of tension.
To probe mechanical sensitivity, we used axon severing and stretching. We found that presynaptic actomyosin and integrin organization respond dynamically to loss and gain of tension.
3/5
Interestingly, depleting neuronal NMII also disrupted postsynaptic NMII organization, pointing to transsynaptic coordination of actomyosin networks.
At the same time, integrin receptors were reduced on both sides of the synapse, indicating compromised neuron–muscle adhesion.
Interestingly, depleting neuronal NMII also disrupted postsynaptic NMII organization, pointing to transsynaptic coordination of actomyosin networks.
At the same time, integrin receptors were reduced on both sides of the synapse, indicating compromised neuron–muscle adhesion.
July 12, 2025 at 9:00 PM
3/5
Interestingly, depleting neuronal NMII also disrupted postsynaptic NMII organization, pointing to transsynaptic coordination of actomyosin networks.
At the same time, integrin receptors were reduced on both sides of the synapse, indicating compromised neuron–muscle adhesion.
Interestingly, depleting neuronal NMII also disrupted postsynaptic NMII organization, pointing to transsynaptic coordination of actomyosin networks.
At the same time, integrin receptors were reduced on both sides of the synapse, indicating compromised neuron–muscle adhesion.
2/5
This linear actin assembly is decorated with nonmuscle myosin II (NMII) and becomes disorganized when NMII is depleted or its activity disrupted—highlighting its reliance on NMII for structural integrity.
This linear actin assembly is decorated with nonmuscle myosin II (NMII) and becomes disorganized when NMII is depleted or its activity disrupted—highlighting its reliance on NMII for structural integrity.
July 12, 2025 at 9:00 PM
2/5
This linear actin assembly is decorated with nonmuscle myosin II (NMII) and becomes disorganized when NMII is depleted or its activity disrupted—highlighting its reliance on NMII for structural integrity.
This linear actin assembly is decorated with nonmuscle myosin II (NMII) and becomes disorganized when NMII is depleted or its activity disrupted—highlighting its reliance on NMII for structural integrity.