The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition

By Jaclyn R. Gareau, C. Lima. Nature reviews. Molecular cell biology, 2010

1,134 citations recorded by the source corpus.

Proteins of the small ubiquitin-related modifier (SUMO) family are conjugated to proteins to regulate such cellular processes as nuclear transport, transcription, chromosome segregation and DNA repair. Recently, numerous insights into regulatory mechanisms of the SUMO modification pathway have emerged. Although SUMO-conjugating enzymes can discriminate between SUMO targets, many substrates possess characteristics that facilitate their modification. Other post-translational modifications also regulate SUMO conjugation, suggesting that SUMO signalling is integrated with other signal transduction pathways. A better understanding of SUMO regulatory mechanisms will lead to improved approaches for analysing the function of SUMO and substrate conjugation in distinct cellular pathways.

Subfields: Molecular Biology, Oncology, Parasitology

View Paper: https://www.semanticscholar.org/paper/891f01f377bc5461c27b820558f7768bf655581a

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Citations in the corpus

• The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “SUMOylation is the process in which SUMO links to a substrate by forming an isopeptide bond between its terminal glycine and the lysine of the substrate.(96,102) Currently, more than 500 substrates have been reported to undergo SUMOylation and take part in regulating the localization, stability and ”