PIAS1 SUMOylates SP3 with SUMO1

Stable Identifier
Reaction [transition]
Homo sapiens
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PIAS1 SUMOylates SP3 with SUMO1 at lysine-551 (Ross et al. 2002, Sapetschnig et al. 2002, Sapetschnig et al. 2004, Spengler et al. 2005, Ellis et al. 2006, Impens et al. 2014). A minor amount of SUMOylation is also observed at lysine-120 (Ross et al. 2002). The effects of SUMOylation on the activities of isoforms of SP3 are promoter-dependent (Sapetschnig et al. 2004). Generally SUMOylation reduces the transcription activation capacity of the long and the short isoforms of Sp3 (Ross et al. 2002, Sapetschnig et al 2004, Ellis et al 2006). Mechanistically, SUMO attachment to Sp3 serves as a molecular beacon for the recruitment of chromatin-modifying machineries that impose epigenetic silencing (inferred from Drosophila homologs in Stielow et al. 2008a, inferred from mouse homologs in Stielow et al. 2008b).
Literature References
PubMed ID Title Journal Year
12356736 Transcription factor Sp3 is silenced through SUMO modification by PIAS1

Sapetschnig, A, Doll, A, Suske, G, Melchior, F, Braun, H, Schergaut, M, Rischitor, G

EMBO J. 2002
18617891 SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing

Sapetschnig, A, Suske, G, Krüger, I, Wink, C, Stielow, B

EMBO Rep. 2008
18374648 Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen

Boutros, M, Brehm, A, Sapetschnig, A, Kunert, N, Suske, G, Krüger, I, Stielow, B

Mol. Cell 2008
15247228 Complexity of translationally controlled transcription factor Sp3 isoform expression

Sapetschnig, A, Koch, F, Suske, G, Mennenga, T, Rischitor, G

J. Biol. Chem. 2004
12419227 SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization

Best, JL, Gill, G, Zon, LI, Ross, S

Mol. Cell 2002
16781829 The modification of Sp3 isoforms by SUMOylation has differential effects on the SRC1A promoter

Ellis, DJ, Dehm, SM, Bonham, K

Gene 2006
25114211 Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli

Impens, F, Cossart, P, Radoshevich, L, Ribet, D

Proc. Natl. Acad. Sci. U.S.A. 2014
15494207 Sumoylation of internally initiated Sp3 isoforms regulates transcriptional repression via a Trichostatin A-insensitive mechanism

Horowitz, JM, Moorefield, KS, Brattain, MG, Kennett, SB, Simmons, SO, Spengler, ML

Cell. Signal. 2005
Event Information
Go Biological Process
Catalyst Activity

SUMO transferase activity of PIAS1 [nucleoplasm]

Orthologous Events
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