First publication of the lab

Better Together: Interorganellar Communication in the Regulation of Proteostasis

I’m thrilled to announce the publication of our latest review, “Better Together: Interorganellar Communication in the Regulation of Proteostasis,” in the journal Contact CTC. This marks the first publication from our lab and my first corresponding review, making it a significant milestone for us.

In this review, we explore the intricate network of chaperones and folding factors that maintain a functional proteome, which is essential for cellular life. Unlike traditional views that isolate proteostatic mechanisms within individual organelles, our review highlights how these processes are interconnected across organellar borders. This interorganellar communication occurs through signaling processes or direct associations via contact sites.

For those interested in the detailed mechanisms and the broader implications of our findings, you can read the full article here

Proteostasis and Aging: Findings from My Postdoctoral Project

I’m pleased to share with you the culmination of my postdoctoral research, a project that has been a significant part of my academic journey. This project, which spanned four years, was centered on the intricate relationship between proteostasis, quiescence, and translation.

The research was conducted during my time as a postdoctoral researcher, a period filled with intense effort, valuable learning experiences, and great collaborative work. I am grateful for the opportunity to work with a team of dedicated individuals, and I appreciate their contributions to this project.

Our findings are now available online and can be accessed here

In our study, we delved into the complex world of cellular proteostasis and its decline with age. This decline leads to protein aggregation, which compromises cell viability. It’s a fascinating and complex process that has significant implications for our understanding of aging and disease. One of our key findings was the role of metabolic cues in aging cells. These cues direct the yeast protein disaggregase Hsp104 to the nucleus. This is a critical process as it helps maintain a functional nuclear proteome during quiescence. In simpler terms, it ensures that the cell’s protein-making machinery remains functional even when the cell is not actively growing or dividing. This mechanism is crucial for the rapid restart of translation when nutrients are available again. It highlights the critical role of cytosolic-nuclear partitioning of Hsp104 in protecting the latent protein synthesis machinery during quiescence in yeast.

As I transition from my research stays in Stockholm and Graz to my new role as an independent group leader in Umeå, I am excited about the future. I look forward to continuing to explore this field and uncovering more of its secrets.

I invite you all to delve into our research and join the conversation. Your thoughts, insights, and questions are most welcome. As we continue to explore this fascinating field, your input can help shape the direction of future research.