SUMO-1 Conjugation in Vivo Requires Both a Consensus Modification Motif and Nuclear Targeting*

By Manuel S. Rodríguez, C. Dargemont, Ronald T. Hay. Journal of Biological Chemistry, 2001

776 citations recorded by the source corpus.

SUMO-1 is a small ubiquitin-related modifier that is covalently linked to many cellular protein targets. Proteins modified by SUMO-1 and the SUMO-1-activating and -conjugating enzymes are located predominantly in the nucleus. Here we define a transferable sequence containing the ΨKXE motif, where Ψ represents a large hydrophobic amino acid, that confers the ability to be SUMO-1-modified on proteins to which it is linked. Whereas addition of short sequences from p53 and IκBα, containing the ΨKXE motif, to a carrier protein is sufficient for modification in vitro, modification in vivorequires the additional presence of a nuclear localization signal. Thus, protein substrates must be targeted to the nucleus to undergo SUMO-1 conjugation.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/bac4848dd40d6646b4d3efbfa0313052c5ab0889

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