Site-specific characterization of endogenous SUMOylation across species and organs
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Site-specific characterization of endogenous SUMOylation across species and organs. / Hendriks, Ivo A.; Lyon, David; Su, Dan; Skotte, Niels H; Daniel, Jeremy A; Jensen, Lars J.; Nielsen, Michael L.
In: Nature Communications, Vol. 9, 2456, 2018, p. 1-17.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Site-specific characterization of endogenous SUMOylation across species and organs
AU - Hendriks, Ivo A.
AU - Lyon, David
AU - Su, Dan
AU - Skotte, Niels H
AU - Daniel, Jeremy A
AU - Jensen, Lars J.
AU - Nielsen, Michael L.
PY - 2018
Y1 - 2018
N2 - Small ubiquitin-like modifiers (SUMOs) are post-translational modifications that play crucial roles in most cellular processes. While methods exist to study exogenous SUMOylation, large-scale characterization of endogenous SUMO2/3 has remained technically daunting. Here, we describe a proteomics approach facilitating system-wide and in vivo identification of lysines modified by endogenous and native SUMO2. Using a peptide-level immunoprecipitation enrichment strategy, we identify 14,869 endogenous SUMO2/3 sites in human cells during heat stress and proteasomal inhibition, and quantitatively map 1963 SUMO sites across eight mouse tissues. Characterization of the SUMO equilibrium highlights striking differences in SUMO metabolism between cultured cancer cells and normal tissues. Targeting preferences of SUMO2/3 vary across different organ types, coinciding with markedly differential SUMOylation states of all enzymes involved in the SUMO conjugation cascade. Collectively, our systemic investigation details the SUMOylation architecture across species and organs and provides a resource of endogenous SUMOylation sites on factors important in organ-specific functions.
AB - Small ubiquitin-like modifiers (SUMOs) are post-translational modifications that play crucial roles in most cellular processes. While methods exist to study exogenous SUMOylation, large-scale characterization of endogenous SUMO2/3 has remained technically daunting. Here, we describe a proteomics approach facilitating system-wide and in vivo identification of lysines modified by endogenous and native SUMO2. Using a peptide-level immunoprecipitation enrichment strategy, we identify 14,869 endogenous SUMO2/3 sites in human cells during heat stress and proteasomal inhibition, and quantitatively map 1963 SUMO sites across eight mouse tissues. Characterization of the SUMO equilibrium highlights striking differences in SUMO metabolism between cultured cancer cells and normal tissues. Targeting preferences of SUMO2/3 vary across different organ types, coinciding with markedly differential SUMOylation states of all enzymes involved in the SUMO conjugation cascade. Collectively, our systemic investigation details the SUMOylation architecture across species and organs and provides a resource of endogenous SUMOylation sites on factors important in organ-specific functions.
U2 - 10.1038/s41467-018-04957-4
DO - 10.1038/s41467-018-04957-4
M3 - Journal article
C2 - 29942033
VL - 9
SP - 1
EP - 17
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 2456
ER -
ID: 198718954