Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 16, Pages 6736-6741Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0810808106
Keywords
activation-induced deaminase; antibody diversification; immunoglobulin class switching; exportin; nuclear transport
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Funding
- FWF Austrian Science [J2508]
- MRC [MC_U105178806] Funding Source: UKRI
- Medical Research Council [MC_U105178806] Funding Source: researchfish
- Austrian Science Fund (FWF) [J2508] Funding Source: Austrian Science Fund (FWF)
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The carboxyterminal region of activation-induced deaminase (AID) is required for its function in Ig class switch recombination (CSR) and also contains a nuclear-export sequence (NES). Here, based on an extensive fine-structure mutation analysis of the AID NES, as well as from AID chimeras bearing heterologous NESs, we show that while a functional NES is indeed essential for CSR, it is not sufficient. The precise nature of the NES is critical both for AID stabilization and CSR function: minor changes in the NES can perturb stabilization and CSR without jeopardizing nuclear export. The results indicate that the AID NES fulfills a function beyond simply providing a signal for nuclear export and suggest the possibility that the quality of exportin-binding may be critical to the stabilization of AID and its activity in CSR.
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