✍️ Author: Dr Eleni Christoforidou
🕒 Approximate reading time: 3 minutes
In our lab’s continuous journey to understand Amyotrophic Lateral Sclerosis (ALS), an intriguing question arose: How do Dynein and TDP-43, two seemingly unrelated proteins, interact in this devastating disease? In our latest research, we dove headfirst into this inquiry, the results of which we’re excited to share with you today.
ALS has long been associated with the protein TDP-43, specifically its propensity to aggregate, or clump together, in neurons. This can disrupt the regular functioning of neurons, leading to the symptoms we associate with ALS. Our recent study explores how Dynein, a motor protein involved in intracellular transport, may play a key role in this aggregation process.
To understand the complexity of our study, you need to envision a city. Now, imagine TDP-43 as residents, and Dynein as the city's transport system. When everything works perfectly, residents (TDP-43) move smoothly through the city (the neuron). However, if there's a problem with the transport system (Dynein), residents may end up where they shouldn't be, causing chaos - in this case, protein aggregation.
To dissect this complex interaction, we looked at the offspring of mice bred to express both human TDP-43 and a mutation in the Dynein gene. The results were intriguing - we observed an increase in TDP-43 aggregation.
This novel finding suggests that defects in Dynein function might contribute to TDP-43 aggregation, leading to ALS symptoms. Thus, understanding this interaction could offer potential avenues for future therapies.
Every study leads to more questions than answers. Our research has opened up a new line of inquiry – how exactly does Dynein influence TDP-43 aggregation? Can we modify this interaction to prevent aggregation and slow down the progression of ALS? As we delve further into these questions, we remain hopeful that our research will contribute to the ongoing fight against this debilitating disease.
Read the original research article here.