In Nature portfolio: Knotty proteins by Maiara Kolbe Musskopf

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PhD student Maiara Kolbe Musskopf participated in the “Science in Shorts” competition organized by Nature portfolio. She had to explain her research in a creative video in less than 1 minute. Her video was selected to be published in the YouTube library of Nature portfolio.
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Intrinsically disordered proteins have important functions, but they can form tangled structures

In the video, Maiara introduces the concept of intrinsically disordered proteins (IDPs), which are very dynamic “spaghetti-like” proteins. IDPs have gained a lot of attention because of their ability to locally and transiently concentrate into what are called condensates, which are extremely important in diverse cellular functions. A big challenge that cells encounter regarding IDPs is the fact that their very dynamic behavior can lead to messy and non-functional protein conglomerates, or aggregates, which can be detrimental to the cellular health and are even involved in certain diseases.

DNAJB6 is an important IDP “untangler”

An example of very important IDPs are the FG-Nups, which populate the central channel of the nuclear pore complex and form a selective barrier for large cargoes that constantly enter and exit the cell nucleus. Previous work from our group showed that the protein DNAJB6 can interact with FG-Nups and prevent them from forming aggregates. This anti-aggregation function of DNAJB6 has also been described for other IDPs, including several ones that cause certain degenerative brain diseases. However, the exact mechanism of DNAJB6 is still unknown.

Untangling the mechanism

DNAJB6 displays a similar anti-aggregation mechanism towards entirely different IDPs, which is not only exciting from a fundamental point of view, but also holds translational potential. By studying the physiological role of DNAJB6 towards FG-Nups, we hope to figure out its mechanism and explore its potential as a means to delay the aggregation and degeneration caused by disease-related IDPs.