6533b823fe1ef96bd127f4fe
RESEARCH PRODUCT
SUMOylation of Blimp-1 promotes its proteasomal degradation
Ari WaismanRivka HadarBoaz TiroshYael DavidLivnat ShimshonStephen L. NuttAvital MichaeliAmi Navonsubject
Proteasome Endopeptidase ComplexSENP1ImmunoprecipitationSUMO-1 ProteinBiophysicsSUMO proteinPlasma cellPlasma cellBiologyBiochemistryCell LineProtein–protein interactionSENP1Structural BiologyEndopeptidasesGeneticsmedicineHumansMolecular BiologyProteasomeProtein StabilityHEK 293 cellsSumoylationCell BiologyCell biologyRepressor ProteinsCysteine Endopeptidasesmedicine.anatomical_structureProteasomeSUMO proteasePositive Regulatory Domain I-Binding Factor 1Intracellulardescription
Abstract B lymphocyte induced maturation protein-1 (Blimp-1) is a transcription repressor of the Krueppel-like family. Blimp-1 plays important roles in developmental processes, such as of germ cells and hair follicle stem cells. In B lymphocytes Blimp-1 orchestrates the terminal differentiation into plasma cells. We discovered that Blimp-1 undergoes SUMOylation by SUMO-1. This SUMOylation is modulated by the SUMO protease SENP1. While Blimp-1 is relatively stable in 293T cells, a fusion with SUMO1 rendered it to rapid proteasomal degradation. Increase in SENP1 activity stabilized Blimp-1, while a decrease promoted its degradation. Our data indicate that SUMOylation of Blimp-1 regulates its intracellular stability. Structured summary of protein interactions Blimp1 physically interacts with SUMO1 by anti tag coimmunoprecipitation (View Interaction 1 , 2 ). SUMO1 physically interacts with Blimp1 by anti tag coimmunoprecipitation (View interaction) .
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2011-06-25 | FEBS Letters |