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| A whole, live cell time-lapse image (2.5 min) of a neuron expressing fluorescently tagged actin (green) and cofilin (red). Credit: Penn State College of Medicine. |
Protein structures are typically determined by studying them in their purified form, outside of the busy inner workings of the cell, and because of this, their biological relevance is often called into question. In a new study by Penn State College of Medicine researchers, the long-observed protein structure cofilactin, a form of the filamentous protein actin that contains numerous connections to cofilin proteins, was shown to be a major component of neuronal growth cone filopodia — small dynamic “antennae” at the tips of growing neurons.
“The effects of cofilin on actin structure and its physical properties have been studied for more than 20 years, but now we can confidently see that this structural alteration serves some biological function in the cell,” said Matt Swulius, assistant professor of biochemistry and molecular biology. “We’re still trying to determine the mechanistic details of its function, but we have strong evidence that cofilactin regulates the flexibility of searching filopodia.”
According to Swulius, understanding how filopodial dynamics are controlled at the molecular level could open therapeutic avenues into nerve regeneration as well as some developmental diseases. His lab is studying how the proteins fascin and cofilin function together to regulate the structure and movement of neuronal filopodia as they navigate their environment to eventually form cellular connections.








