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Sumoylation regulates nuclear localization of repressor DREAM

AutorPalczewska, Malgorzata; Casafont, Íñigo; Ghimire, Kedar; Rojas, A. M. ; Valencia, Alfonso; Lafarga, Miguel; Mellström, Britt; Naranjo, José Ramón
Palabras claveDREAM
KChIPs
Nuclear localization
SUMO
Ubc9
Trigeminal neuron
Fecha de publicaciónmay-2011
EditorElsevier
CitaciónBiochimica et Biophysica Acta - Molecular Cell Research 1813(5): 1050-1058 (2011)
ResumenDREAM is a Ca2+-binding protein with specific functions in different cell compartments. In the nucleus, DREAM acts as a transcriptional repressor, although the mechanism that controls its nuclear localization is unknown. Yeast two-hybrid assay revealed the interaction between DREAM and the SUMO-conjugating enzyme Ubc9 and bioinformatic analysis identified four sumoylation-susceptible sites in the DREAM sequence. Single K-to-R mutations at positions K26 and K90 prevented in vitro sumoylation of recombinant DREAM. DREAM sumoylation mutants retained the ability to bind to the DRE sequence but showed reduced nuclear localization and failed to regulate DRE-dependent transcription. In PC12 cells, sumoylated DREAM is present exclusively in the nucleus and neuronal differentiation induced nuclear accumulation of sumoylated DREAM. In fully differentiated trigeminal neurons, DREAM and SUMO-1 colocalized in nuclear domains associated with transcription. Our results show that sumoylation regulates the nuclear localization of DREAM in differentiated neurons. This article is part of a Special Issue entitled: 11th European Symposium on Calcium.
Versión del editorhttps://doi.org/10.1016/j.bbamcr.2010.11.001
URIhttp://hdl.handle.net/10261/153619
DOI10.1016/j.bbamcr.2010.11.001
ISSN0167-4889
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