Reactome | SUMOylation of BLM with SUMO2,3

SUMOylation of BLM with SUMO2,3

Stable Identifier

R-HSA-4568914

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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BLM is SUMOylated at lysine-317, lysine-331, lysine-344, and lysine-347 with SUMO2,3 (Eladad et al. 2005, Zhu et al. 2008, Ouyang et al. 2009, Ouyang et al. 2013, Hendriks et al. 2014). SUMOylation causes BLM to localize to PML bodies (Eladad et al. 2005). SUMOylated BLM recruits RAD51, which directly binds SUMO, and facilitates the substitution of RAD51 for RPA at stalled replication forks (Ouyang et al. 2009, 2013).

Literature References

PubMed ID	Title	Journal	Year
15829507	Intra-nuclear trafficking of the BLM helicase to DNA damage-induced foci is regulated by SUMO modification Eladad, S, Ye, TZ, Hu, P, Leversha, M, Beresten, S, Matunis, MJ, Ellis, NA	Hum. Mol. Genet.	2005
25218447	Uncovering global SUMOylation signaling networks in a site-specific manner Hendriks, IA, D'Souza, RC, Yang, B, Verlaan-de Vries, M, Mann, M, Vertegaal, AC	Nat. Struct. Mol. Biol.	2014
18708356	Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification Zhu, J, Zhu, S, Guzzo, CM, Ellis, NA, Sung, KS, Choi, CY, Matunis, MJ	J. Biol. Chem.	2008
24027577	BLM SUMOylation regulates ssDNA accumulation at stalled replication forks Ouyang, KJ, Yagle, MK, Matunis, MJ, Ellis, NA	Front Genet	2013
19956565	SUMO modification regulates BLM and RAD51 interaction at damaged replication forks Ouyang, KJ, Woo, LL, Zhu, J, Huo, D, Matunis, MJ, Ellis, NA	PLoS Biol.	2009