Short talk:
A possible role of the ubiquitin kinase PINK1 in protein quality control

Linlin Lei1, Koustav Ray1, Jörg Tatzelt2,3, Konstanze F. Winklhofer1,3

1Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801 Bochum, Germany.
2Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801 Bochum, Germany.
3RESOLV Cluster of Excellence, Ruhr University Bochum, 44801 Bochum,

Degradation of dysfunctional, damaged, or misfolded proteins is a crucial component of the protein quality control network to maintain cellular proteostasis. Dysfunction in proteostasis regulation due to imbalances in protein synthesis, folding, and degradation challenges the integrity of the cellular proteome and favors the accumulation of aggregated proteins that can damage cells by a loss of their functions and/or a gain of adverse functions. Ubiquitination is an essential player in proteostasis regulation but also in orchestrating signaling pathways in response to various stress conditions. Both cellular degradation systems, the proteasome and autophagy, employ ubiquitin for selection and targeting of substrates to the degradative machineries. We recently found that linear ubiquitin chains generated by LUBAC are implicated in the clearance of protein aggregates associated with neurodegenerative diseases, such as Huntington’s disease or Parkinson’s disease. In this study, we are analyzing a possible role of PINK1 in protein quality control, based on our observation that PINK1 is co-localizing with pathogenic protein aggregates.

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