Catching proteins for degradation

Article Multidisciplinary Sciences

The midnolin-proteasome pathway catches proteins for ubiquitination-independent degradation

Xin Gu et al.

Summary: Cells use ubiquitin to mark proteins for degradation, but the mechanism for the degradation of some proteins is unclear. This study found that midnolin promotes the degradation of nuclear proteins by binding to the proteasome, binding to substrates, and using a ubiquitin-like domain to promote substrate degradation.

SCIENCE (2023)

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Review Biochemistry & Molecular Biology

UBQLN proteins in health and disease with a focus on UBQLN2 in ALS/FTD

Brian C. Lin et al.

Summary: Ubiquilin (UBQLN) proteins are a versatile family of proteins found in all eukaryotes, with emerging evidence suggesting broader roles in proteostasis beyond their canonical function as shuttle factors. Understanding the different roles of UBQLN proteins, how changes in their structure regulate activity, and the pathogenic mechanisms of UBQLN2 mutations provide fundamental insight into disease pathogenesis through proteostasis disturbances.

FEBS JOURNAL (2022)

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Review Biochemistry & Molecular Biology

Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies

Xiang Chen et al.

Summary: The 26S proteasome is responsible for regulated proteolysis in eukaryotic cells, with substrates targeted to it through post-translational modification with ubiquitin. Deubiquitinating enzymes (DUBs) play a crucial role in catalyzing ubiquitin chain hydrolysis, coupling deubiquitination to substrate unfolding and degradation. This intricate machinery of proteasomes and ubiquitin-modified substrates remains an active area of investigation, with potential for therapeutic targeting.

FEBS JOURNAL (2021)

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Article Multidisciplinary Sciences