Serum response factor is modulated by the SUMO-1 conjugation system.
Serum stimulation leads to activation of the serum response factor (SRF)-mediated transcription of immediate-early genes such as c-fos via various signal transduction pathways. We have previously reported that promyelocytic leukemia protein (PML) is involved in the transcriptional regulation by SRF. PML is one of the well-known substrates for modification by ... small ubiquitin-related modifier-1 (SUMO-1) and several SUMO-1-modified proteins associate with PML. Here, we report that SRF is modified by SUMO-1 chiefly at lysine(147) within the DNA-binding domain. Substitution of this target lysine for alanine did not affect the translocation of SRF to PML-nuclear bodies. The SRF mutant augmented the transcriptional activity under Rho A-stimulated condition but not under serum-starved condition, suggesting that activated SRF is suppressed by its sumoylation. These data support the transcriptional role of SUMO-1 conjugating system in cellular serum response.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, DNA, Complementary, HeLa Cells, Humans, Lysine, Neoplasm Proteins, Nuclear Proteins, Protein Processing, Post-Translational, Protein Structure, Tertiary, Recombinant Proteins, SUMO-1 Protein, Serum Response Factor, Transcription Factors, Transcription, Genetic, Tumor Suppressor Proteins
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, DNA, Complementary, HeLa Cells, Humans, Lysine, Neoplasm Proteins, Nuclear Proteins, Protein Processing, Post-Translational, Protein Structure, Tertiary, Recombinant Proteins, SUMO-1 Protein, Serum Response Factor, Transcription Factors, Transcription, Genetic, Tumor Suppressor Proteins
Biochem. Biophys. Res. Commun.
Date: Jun. 20, 2003
PubMed ID: 12788062
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