RSUME, a Small RWD-Containing Protein, Enhances SUMO Conjugation and Stabilizes HIF-1α during Hypoxia
SUMO conjugation to proteins is involved in the regulation of diverse cellular functions. We have identified a protein, RWD-containing sumoylation enhancer (RSUME), that enhances overall SUMO-1, -2, and -3 conjugation by interacting with the SUMO conjugase Ubc9. RSUME increases noncovalent binding o...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2007 |
| País: | Argentina |
| Institución: | Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
| Repositorio: | Biblioteca Digital (UBA-FCEN) |
| Idioma: | inglés |
| OAI Identifier: | paperaa:paper_00928674_v131_n2_p309_CarbiaNagashima |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00928674_v131_n2_p309_CarbiaNagashima |
| Access Level: | acceso abierto |
| Palabra clave: | CELLBIO PROTEINS cell protein hypoxia inducible factor 1alpha I kappa B immunoglobulin enhancer binding protein protein RSUME protein Ubc9 SUMO 1 protein sumo 2 protein sumo 3 protein SUMO protein unclassified drug animal cell article cell function conjugation controlled study genetic transcription human human cell hypoxia mammal cell mouse nonhuman nucleotide sequence polymerization priority journal protein binding protein domain protein expression protein protein interaction protein stability protein structure rat regulatory mechanism sumoylation Amino Acid Sequence Animals Base Sequence Cell Hypoxia Cell Line, Tumor Cercopithecus aethiops Humans Hypoxia-Inducible Factor 1, alpha Subunit I-kappa B Kinase Molecular Sequence Data NF-kappa B Organ Specificity Protein Binding Small Ubiquitin-Related Modifier Proteins SUMO-1 Protein Transcription Factors Ubiquitin-Conjugating Enzymes Ubiquitins Mammalia |
| Sumario: | SUMO conjugation to proteins is involved in the regulation of diverse cellular functions. We have identified a protein, RWD-containing sumoylation enhancer (RSUME), that enhances overall SUMO-1, -2, and -3 conjugation by interacting with the SUMO conjugase Ubc9. RSUME increases noncovalent binding of SUMO-1 to Ubc9 and enhances Ubc9 thioester formation and SUMO polymerization. RSUME enhances the sumoylation of IkB in vitro and in cultured cells, leading to an inhibition of NF-kB transcriptional activity. RSUME is induced by hypoxia and enhances the sumoylation of HIF-1α, promoting its stabilization and transcriptional activity during hypoxia. Disruption of the RWD domain structure of RSUME demonstrates that this domain is critical for RSUME action. Together, these findings point to a central role of RSUME in the regulation of sumoylation and, hence, several critical regulatory pathways in mammalian cells. © 2007 Elsevier Inc. All rights reserved. |
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