Dr. Wolfgang Girzalsky, Prof. Dr. Ralf Erdmann, and Dr. Ismaila Francis Yusuf (from left) study cellular processes in yeast. 

© RUB, Kramer

Biochemistry

New Quality Control Discovered in Yeast Peroxisomes

Researchers have identified a previously unknown mechanism for maintaining cell function.

Peroxisomes are essential cell organelles that play a vital role in lipid metabolism and cellular detoxification. To perform these functions, numerous enzymes must be correctly transported into the organelles. A research team at Ruhr University Bochum, Germany, led by Professor Ralf Erdmann and Dr. Ismaila Francis Yusuf has now discovered a previously unknown quality control mechanism that governs peroxisomal protein transport in the baker’s yeast Saccharomyces cerevisiae. This mechanism is crucial for maintaining peroxisomal function. The study was published in Cell Reports on October 28, 2025.

Finding and breaking down defective proteins

For the first time, the researchers have identified and molecularly characterized the RADAR pathway (“Receptor Accumulation and Degradation in the Absence of Recycling”) in baker’s yeast. This mechanism ensures that import receptors that are defective or no longer functional are specifically recognized, tagged, and degraded. “This prevents faulty proteins from interfering with the function of peroxisomes,” explains Ralf Erdmann, Chair of the Department of Systems Biochemistry at Ruhr University Bochum.

The Bochum-based team of authors: Wolfgang Girzalsky, Ismaila Francis Yusuf, the lead author of the paper, and Ralf Erdmann (from left to right)

© RUB, Kramer

At the core of the RADAR pathway is the AAA-ATPase Cdc48p, which orchestrates the degradation process together with its cofactors Ufd1p and Npl4p, as well as the AAA-ATPase Msp1p. The researchers demonstrated that Cdc48p extracts defective import receptors from the peroxisomal membrane, enabling their subsequent degradation by the proteasome. Thus, the RADAR pathway resembles the well-characterized ERAD system (Endoplasmic Reticulum-Associated Degradation), which fulfills a comparable quality control function in the endoplasmic reticulum. 

Contribution to cell health

“Our results show that peroxisomes possess a specialized quality control mechanism that prevents malfunctions and supports cellular health,” explains Erdmann. “This discovery represents a major step forward in understanding peroxisomal quality control and the role of Cdc48p in cellular protein surveillance.” Because peroxisomes play a central role in human metabolism and the RADAR pathway is conserved in humans, these findings offer new insights into the fundamental mechanisms of cellular homeostasis and protein quality control.

Original publication

Ismaila Francis Yusuf, Tomasz Jeziorek, Andrea Droste, Wolfgang Girzalski, Ralf Erdmann: Role of AAA-ATPase Cdc48p in Peroxisomal Quality Control, in Cell Reports, 2025, DOI: 10.1016/j.celrep.2025.116405

Press contact

Professor Ralf Erdmann
Department of Systems Biochemistry
Institute of Biochemistry and Pathobiochemistry
Faculty of Medicine
Ruhr University Bochum
Germany
Email: ralf.erdemann@ruhr-uni-bochum.de 

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Published

Wednesday
29 October 2025
9:35 am

By

Meike Drießen (md)

Translated by

allround Fremdsprachen GmbH von der Lühe

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