Dataset Information


Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification.

ABSTRACT: Small ubiquitin-related modifiers (SUMOs) regulate diverse cellular processes through their covalent attachment to target proteins. Vertebrates express three SUMO paralogs: SUMO-1, SUMO-2, and SUMO-3 (SUMO-2 and SUMO-3 are approximately 96% identical and referred to as SUMO-2/3). SUMO-1 and SUMO-2/3 are conjugated, at least in part, to unique subsets of proteins and thus regulate distinct cellular pathways. However, how different proteins are selectively modified by SUMO-1 and SUMO-2/3 is unknown. We demonstrate that BLM, the RecQ DNA helicase mutated in Bloom syndrome, is preferentially modified by SUMO-2/3 both in vitro and in vivo. Our findings indicate that non-covalent interactions between SUMO and BLM are required for modification at non-consensus sites and that preferential SUMO-2/3 modification is determined by preferential SUMO-2/3 binding. We also present evidence that sumoylation of a C-terminal fragment of HIPK2 is dependent on SUMO binding, indicating that non-covalent interactions between SUMO and target proteins provide a general mechanism for SUMO substrate selection and possible paralog-selective modification.


PROVIDER: S-EPMC2570875 | BioStudies | 2008-01-01T00:00:00Z

REPOSITORIES: biostudies

Similar Datasets

1000-01-01 | S-EPMC4086084 | BioStudies
2010-01-01 | S-EPMC2892505 | BioStudies
1000-01-01 | S-EPMC5660086 | BioStudies
2008-01-01 | S-EPMC2525526 | BioStudies
2009-01-01 | S-EPMC2794540 | BioStudies
2002-01-01 | S-EPMC135644 | BioStudies
2009-01-01 | S-EPMC2779653 | BioStudies
2017-01-01 | S-EPMC5602394 | BioStudies
2015-01-01 | S-EPMC4445636 | BioStudies
2008-01-01 | S-EPMC2390597 | BioStudies