SUMOylation of blimp-1 promotes its proteasomal degradation

Livnat Shimshon, Avital Michaeli, Rivka Hadar, Stephen L. Nutt, Yael David, Ami Navon, Ari Waisman, Boaz Tirosh*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

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).

Original languageAmerican English
Pages (from-to)2405-2409
Number of pages5
JournalFEBS Letters
Volume585
Issue number15
DOIs
StatePublished - 4 Aug 2011

Bibliographical note

Funding Information:
This work was supported by grants from the German Israel Foundation 1005/08 (BT and AW). The authors wish to declare no financial conflict of interests.

Keywords

  • Plasma cell
  • Proteasome
  • SENP1
  • SUMO protease

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