The Trinity of SPRTN Protease Regulation

Annamaria Ruggiano; Kristijan Ramadan

doi:10.1016/j.tibs.2020.10.007

The Trinity of SPRTN Protease Regulation

Trends Biochem Sci. 2021 Jan;46(1):2-4. doi: 10.1016/j.tibs.2020.10.007. Epub 2020 Nov 9.

Authors

Annamaria Ruggiano¹, Kristijan Ramadan²

Affiliations

¹ Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Roosevelt Drive, OX3 7DQ, Oxford, UK.
² Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Roosevelt Drive, OX3 7DQ, Oxford, UK. Electronic address: kristijan.ramadan@oncology.ox.ac.uk.

PMID: 33183910
DOI: 10.1016/j.tibs.2020.10.007

Abstract

The protease SPRTN emerged as the essential enzyme for DNA-protein crosslink proteolysis repair. Biochemical and cell biological work indicated that SPRTN is a nonspecific protease. Recent and independent studies from Lou, Stingele, and Ramadan reveal that SPRTN activity is modulated via three layers of regulation that make it selective for DNA-protein crosslinks.

Keywords: DNA–protein crosslinks; SPRTN protease; cancer; genomic instability.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

DNA-Binding Proteins / metabolism*
Humans

Substances

DNA-Binding Proteins
SPRTN protein, human

Abstract

Publication types

MeSH terms

Substances

Grants and funding