| The dependence of Ig class-switching on the nuclear export sequence of AID likely reflects interaction with factors additional to Crm1 exportin. | |
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MedLine Citation:
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PMID: 21268017 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Activation-induced deaminase (AID) is a B lymphocyte-specific DNA deaminase that triggers Ig class-switch recombination (CSR) and somatic hypermutation. It shuttles between cytoplasm and nucleus, containing a nuclear export sequence (NES) at its carboxyterminus. Intriguingly, the precise nature of this NES is critical to AID's function in CSR, though not in somatic hypermutation. Many alterations to the NES, while preserving its nuclear export function, destroy CSR ability. We have previously speculated that AID's ability to potentiate CSR may critically depend on the affinity of interaction between its NES and Crm1 exportin. Here, however, by comparing multiple AID NES mutants, we find that - beyond a requirement for threshold Crm1 binding - there is little correlation between CSR and Crm1 binding affinity. The results suggest that CSR, as well as the stabilisation of AID, depend on an interaction between the AID C-terminal decapeptide and factor(s) additional to Crm1. |
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Authors:
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Julia I Ellyard; Amelie S Benk; Benjamin Taylor; Cristina Rada; Michael S Neuberger |
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Publication Detail:
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Type: Journal Article Date: 2010-12-23 |
Journal Detail:
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Title: European journal of immunology Volume: 41 ISSN: 1521-4141 ISO Abbreviation: Eur. J. Immunol. Publication Date: 2011 Feb |
Date Detail:
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Created Date: 2011-01-26 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 1273201 Medline TA: Eur J Immunol Country: Germany |
Other Details:
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Languages: eng Pagination: 485-90 Citation Subset: IM |
Copyright Information:
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Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
Affiliation:
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Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, UK. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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