The SUMO Isopeptidase SENP6 Functions as a Rheostat of Chromatin Residency in Genome Maintenance and Chromosome Dynamics.

Signaling by the ubiquitin-related SUMO pathway relies on coordinated conjugation and deconjugation events. SUMO-specific deconjugating enzymes counterbalance SUMOylation, but comprehensive insight into their substrate specificity and regulation is missing. By characterizing SENP6, we define an N-terminal multi-SIM domain as a critical determinant in targeting SENP6 to SUMO chains.

Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling.

Attachment of SUMO to proteins regulates protein-protein interactions through noncovalent binding of the SUMO moiety to specialized SUMO interaction motifs (SIMs). A core of hydrophobic amino acids has been described as the major determinant of SIM function. Using the transcriptional coregulator and SUMO ligase PIAS1 as a model, we define an extended phospho-regulated SIM module.

Regulation of p53 family members by the ubiquitin-like SUMO system.

p53 and its cousins p63 and p73 are critical regulators of the genotoxic stress response in mammalian cells. Their activity is controlled by an intricate network of post-translational modifications. The ubiquitin-like SUMO system targets all three family members and modulates their transcriptional activity, stability or subcellular trafficking.

In vivo production of artificial nonribosomal peptide products in the heterologous host Escherichia coli.

Nonribosomal peptide synthetases represent the enzymatic assembly lines for the biosynthesis of pharmacologically relevant natural peptides, e.g., cyclosporine, vancomycin, and penicillin.