About

The Autophagy Research Group performs basic research with a main focus on the molecular mechanisms and roles of selective autophagy in cell signaling and disease mechanisms.

Following our discovery of the first mammalian selective autophagy receptors p62/SQSTM1 and NBR1 we have focused our research on autophagy and particularly selective autophagy. Autophagy is an evolutionary conserved renovation process in cells, acting as a key regulator of cell survival or death in response to a variety of internal and external signals. Our work on the scaffold and signaling protein p62/SQSTM1 led to the discovery of autophagy receptors that specifically direct protein aggregates, organelles, nucleic acids, and pathogens for degradation.
^{Steps in the (macro)autophagy process}

Disabled autophagy plays a major role in human diseases including cancer, heart failure, metabolic, inflammatory, and neurodegenerative diseases. Specific protein-protein interactions and their functional consequences are being addressed in all projects using a set of biochemical-, cell biological- and immunological tools. Bioimaging and Proteomics are important in the research strategy of the group. Our research is funded by the Norwegian Cancer Society and the Research Council of Norway in addition to the support we receive from UiT.

Autophagy Research Group Anno 2022

Research Impact

• Discovered the first selective autophagy receptors p62/SQSTM1 and NBR1
• Showed that the selective autophagy receptors bound to cargo and to Atg8 family proteins
• Identified the LIR motif mediating the interaction in the majority of Atg8 interacting proteins
• Discovered p62 formed protein bodies inside cells that are degraded by autophagy
• Developed a novel tandem tag fluorescent protein assay to monitor autophagic flux
• Described the positive feedback loop regulation between p62 and NRF2
• Found NBR1 as the selective autophagy receptor in plants
• Discovered NBR1 acting as a pexophagy receptor
• Discovered the first Golgiphagy receptor, CALCOCO1, also acting in ERphagy
• Showed Atg8 family proteins to act as membrane-bound scaffolds for autophagy core machinery proteins including the ULK1/2 complexes, the PI3K class III complex and ATG4 proteins.
• Showed NIPSNAP1 and NIPSNAP2 to act as "Eat Me" signals for Mitophagy
• Discovered that FKBP8 can act as a mitophagy receptor and that SAMM50 is involved in basal and OXPHOS-induced mitophagy
• Found the inflammation repressor TNIP1/ABIN-1 to be degraded by autophagy following TBK1 activation.