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Reference: Moutty MC, et al. (2011) Importin α/{beta} mediates nuclear import of individual SUMO E1 subunits and of the holo-enzyme. Mol Biol Cell 22(5):652-60

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Abstract

SUMOylation, reversible attachment of small ubiquitin-related modifier (SUMO), serves to regulate hundreds of proteins. Consistent with predominantly nuclear targets, enzymes required for attachment and removal of SUMO are highly enriched in this compartment. This is true also for the first enzyme of the sumoylation cascade, the SUMO E1 enzyme heterodimer, Aos1/Uba2 (SAE1/SAE2). This essential enzyme serves to activate SUMO and to transfer it to the E2 conjugating enzyme Ubc9. While the last 40 amino acids in yeast Uba2 have been implicated in its nuclear localization, little was known about the import pathways of Aos1, Uba2 and/or of the assembled E1 heterodimer. Here we show that the mammalian E1 subunits can be imported separately, identify nuclear import signals (NLSs) in Aos1 and in Uba2, and demonstrate that their import is mediated by importin alpha/beta in vitro and in intact cells. Once assembled into a stable heterodimer, the E1 enzyme can still be efficiently imported by importin alpha/beta, due to the Uba2 NLS that is still accessible. These pathways may serve distinct purposes, import of nascent subunits prior to assembly, and re-import of stable E1 enzyme complex after mitosis.

Reference Type
Journal Article
Authors
Moutty MC, Sakin V, Melchior F
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