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Fancm-deficient mice reveal unique features of Fanconi anemia complementation group M

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Fancm-deficient mice reveal unique features of Fanconi anemia complementation group M

Abstract

Abstract The Fanconi anemia (FA) core complex member FANCM remodels synthetic replication forks and recombination intermediates. Thus far, only one FA patient with FANCM mutations has been described, but the relevance of these mutations for the FA phenotype is uncertain. To provide further experimental access to the FA-M complementation group we have generated Fancm- deficient mice by deleting exon 2. FANCM deficiency caused hypogonadism in mice and hypersensitivity to cross-linking agents in mouse embryonic fibroblasts (MEFs), thus phenocopying other FA mouse models. However, Fancm Δ2/Δ2 mice also showed unique features atypical for FA mice, including underrepresentation of female Fancm Δ2/Δ2 mice and decreased overall and tumor-free survival. This increased cancer incidence may be correlated to the role of FANCM in the suppression of spontaneous sister chromatid exchanges as observed in MEFs. In addition, FANCM appeared to have a stimulatory rather than essential role in FANCD2 monoubiquitination. The FA-M mouse model presented here suggests that FANCM functions both inside and outside the FA core complex to maintain genome stability and to prevent tumorigenesis. © The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
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Title
Fancm-deficient mice reveal unique features of Fanconi anemia complementation group M
Author(s)
Bakker, Sietske T.; van de Vrugt, Henri J.; Rooimans, Martin A.; Oostra, Anneke B.; Steltenpool, Jurgen; Delzenne-Goette, Elly; van der Wal, Anja; van der Valk, Martin; Joenje, Hans; te Riele, Hein; de Winter, Johan P.
Journal
Human Molecular Genetics , Volume 18 (18): 3484 Oxford University Press – Sep 15, 2009
Publisher
Oxford University Press
Copyright
Copyright © 2010 Oxford University Press
ISSN
0964-6906
eISSN
1460-2083
D.O.I.
10.1093/hmg/ddp297
Publisher site
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