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Publication : The uncharacterized SANT and BTB domain-containing protein SANBR inhibits class switch recombination.

First Author  Zheng S Year  2021
Journal  J Biol Chem Volume  296
Pages  100625 PubMed ID  33831416
Mgi Jnum  J:322384 Mgi Id  MGI:6707280
Doi  10.1016/j.jbc.2021.100625 Citation  Zheng S, et al. (2021) The uncharacterized SANT and BTB domain-containing protein SANBR inhibits class switch recombination. J Biol Chem :100625
abstractText  Class switch recombination (CSR) is the process by which B cells switch production from IgM/IgD to other immunoglobulin isotypes, enabling them to mount an effective immune response against pathogens. Timely resolution of CSR prevents damage due to an uncontrolled and prolonged immune response. While many positive regulators of CSR have been described, negative regulators of CSR are relatively unknown. Using an shRNA library screen targeting more than 28,000 genes in a mouse B cell line, we have identified a novel, uncharacterized protein of 82kD (KIAA1841, NM_027860), which we have named SANBR (SANT and BTB domain regulator of CSR), as a negative regulator of CSR. The purified, recombinant BTB domain of SANBR exhibited characteristic properties such as homodimerization and interaction with co-repressor proteins, including HDAC and SMRT. Overexpression of SANBR inhibited CSR in primary mouse splenic B cells, and inhibition of CSR is dependent on the BTB domain while the SANT domain is largely dispensable. Thus, we have identified a new member of the BTB family that serves as a negative regulator of CSR. Future investigations to identify transcriptional targets of SANBR in B cells will reveal further insights into the specific mechanisms by which SANBR regulates CSR as well as fundamental gene regulatory activities of this protein.
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