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Specification of SUMO1- and SUMO2-interacting Motifs

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Hecker, Christina-Maria, Rabiller, Matthias, Haglund, Kaisa, Bayer, Peter, Dikic, Ivan·2006·Journal of Biological Chemistry

Abstract

SUMO proteins are ubiquitin-related modifiers implicated in the regulation of gene transcription, cell cycle, DNA repair, and protein localization. The molecular mechanisms by which the sumoylation of target proteins regulates diverse cellular functions remain poorly understood. Here we report isolation and characterization of SUMO1- and SUMO2-binding motifs. Using yeast two-hybrid system, bioinformatics, and NMR spectroscopy we define a common SUMO-interacting motif (SIM) and map its binding surfaces on SUMO1 and SUMO2. This motif forms a beta-strand that could bind in parallel or antiparallel orientation to the beta2-strand of SUMO due to the environment of the hydrophobic core. A negative charge imposed by a stretch of neighboring acidic amino acids and/or phosphorylated serine residues determines its specificity in binding to distinct SUMO paralogues and can modulate the spatial orientation of SUMO-SIM interactions.

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Metadata

Authors
Hecker, C.-M., Rabiller, M., Haglund, K., Bayer, P., & Dikic, I.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2006-06
Volume
281
Issue
23
Pages
16117-16127
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2070182263
Cited by
587
References
0
FWCI
13.02
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Specification of SUMO1- and SUMO2-interacting Motifs. https://app.cochat.ai/papers/10.1074/jbc.m512757200
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Hecker, C.-M., Rabiller, M., Haglund, K., Bayer, P., & Dikic, I. (2006). Specification of SUMO1- and SUMO2-interacting Motifs. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m512757200

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.