RSUME, a Small RWD-Containing Protein, Enhances SUMO Conjugation and Stabilizes HIF-1α during Hypoxia

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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...

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Detalles Bibliográficos
Autores principales: Carbia-Nagashima, A., Gerez, J., Perez-Castro, C., Paez-Pereda, M., Silberstein, S., Stalla, G.K., Holsboer, F., Arzt, E.
Formato: Artículo publishedVersion
Publicado: 2007
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00928674_v131_n2_p309_CarbiaNagashima
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00928674_v131_n2_p309_CarbiaNagashima_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires
Descripción
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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