TY  - JOUR
A1  - Hecker, Christina-Maria
A1  - Rabiller, Matthias
A1  - Haglund, Kaisa
A1  - Bayer, Peter
A1  - Đikić, Ivan
T1  - Specification of SUMO1- and SUMO2-interacting motifs
T2  - Journal of biological chemistry
N2  - 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.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76261
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-762612
SN  - 0021-9258
VL  - 281.2006
IS  - 23, art. 16127
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -