The splicing regulator PTBP2 interacts with the cytidine deaminase AID and promotes binding of AID to switch-region DNA Journal Article


Authors: Nowak, U.; Matthews, A. J.; Zheng, S.; Chaudhuri, J.
Article Title: The splicing regulator PTBP2 interacts with the cytidine deaminase AID and promotes binding of AID to switch-region DNA
Abstract: During immunoglobulin class-switch recombination (CSR), the cytidine deaminase AID induces double-strand breaks into transcribed, repetitive DNA elements called switch sequences. The mechanism that promotes the binding of AID specifically to switch regions remains to be elucidated. Here we used a proteomic screen with in vivo biotinylation of AID to identify the splicing regulator PTBP2 as a protein that interacts with AID. Knockdown of PTBP2 mediated by short hairpin RNA in B cells led to a decrease in binding of AID to transcribed switch regions, which resulted in considerable impairment of CSR. PTBP2 is thus an effector of CSR that promotes the binding of AID to switch-region DNA. © 2011 Nature America, Inc. All rights reserved.
Keywords: unclassified drug; nonhuman; protein function; protein dna binding; protein protein interaction; proteomics; dna strand breakage; gene rearrangement; genetic recombination; cytidine deaminase; enzyme analysis; regulator protein; biotinylation; protein aid; protein ptbp2
Journal Title: Nature Immunology
Volume: 12
Issue: 2
ISSN: 1529-2908
Publisher: Nature Publishing Group  
Date Published: 2011-02-01
Start Page: 160
End Page: 166
Language: English
DOI: 10.1038/ni.1977
PROVIDER: scopus
PUBMED: 21186367
PMCID: PMC3724472
DOI/URL:
Notes: --- - "Export Date: 4 March 2011" - "CODEN: NIAMC" - "Source: Scopus"
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