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FANCD2 Binds CtIP and Regulates DNA-End Resection during DNA Interstrand Crosslink Repair

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Title: FANCD2 Binds CtIP and Regulates DNA-End Resection during DNA Interstrand Crosslink Repair
Authors: Junya Unno, Akiko Itaya, Masato Taoka, Koichi Sato, Junya Tomida, Wataru Sakai, Kaoru Sugasawa, Masamichi Ishiai, Tsuyoshi Ikura, Toshiaki Isobe, Hitoshi Kurumizaka, Minoru Takata
Source: Cell Reports, Vol 7, Iss 4, Pp 1039-1047 (2014)
Publisher Information: Elsevier, 2014.
Publication Year: 2014
Collection: LCC:Biology (General)
Subject Terms: Biology (General), QH301-705.5
More Details: The Fanconi anemia (FA) pathway is critically involved in the maintenance of hematopoietic stem cells and the suppression of carcinogenesis. A key FA protein, FANCD2, is monoubiquitinated and accumulates in chromatin in response to DNA interstrand crosslinks (ICLs), where it coordinates DNA repair through mechanisms that are still poorly understood. Here, we report that CtIP protein directly interacts with FANCD2. A region spanning amino acids 166 to 273 of CtIP and monoubiquitination of FANCD2 are both essential for the FANCD2-CtIP interaction and mitomycin C (MMC)-induced CtIP foci. Remarkably, both FANCD2 and CtIP are critical for MMC-induced RPA2 hyperphosphorylation, an event that accompanies end resection of double-strand breaks. Collectively, our results reveal a role of monoubiquitinated FANCD2 in end resection that depends on its binding to CtIP during ICL repair.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2211-1247
Relation: http://www.sciencedirect.com/science/article/pii/S2211124714002927; https://doaj.org/toc/2211-1247
DOI: 10.1016/j.celrep.2014.04.005
Access URL: https://doaj.org/article/e36387d2c5d74315a6dd602ff2eac987
Accession Number: edsdoj.36387d2c5d74315a6dd602ff2eac987
Database: Directory of Open Access Journals
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  Data: FANCD2 Binds CtIP and Regulates DNA-End Resection during DNA Interstrand Crosslink Repair
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  Data: <searchLink fieldCode="AR" term="%22Junya+Unno%22">Junya Unno</searchLink><br /><searchLink fieldCode="AR" term="%22Akiko+Itaya%22">Akiko Itaya</searchLink><br /><searchLink fieldCode="AR" term="%22Masato+Taoka%22">Masato Taoka</searchLink><br /><searchLink fieldCode="AR" term="%22Koichi+Sato%22">Koichi Sato</searchLink><br /><searchLink fieldCode="AR" term="%22Junya+Tomida%22">Junya Tomida</searchLink><br /><searchLink fieldCode="AR" term="%22Wataru+Sakai%22">Wataru Sakai</searchLink><br /><searchLink fieldCode="AR" term="%22Kaoru+Sugasawa%22">Kaoru Sugasawa</searchLink><br /><searchLink fieldCode="AR" term="%22Masamichi+Ishiai%22">Masamichi Ishiai</searchLink><br /><searchLink fieldCode="AR" term="%22Tsuyoshi+Ikura%22">Tsuyoshi Ikura</searchLink><br /><searchLink fieldCode="AR" term="%22Toshiaki+Isobe%22">Toshiaki Isobe</searchLink><br /><searchLink fieldCode="AR" term="%22Hitoshi+Kurumizaka%22">Hitoshi Kurumizaka</searchLink><br /><searchLink fieldCode="AR" term="%22Minoru+Takata%22">Minoru Takata</searchLink>
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  Data: Cell Reports, Vol 7, Iss 4, Pp 1039-1047 (2014)
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  Data: Elsevier, 2014.
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  Label: Description
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  Data: The Fanconi anemia (FA) pathway is critically involved in the maintenance of hematopoietic stem cells and the suppression of carcinogenesis. A key FA protein, FANCD2, is monoubiquitinated and accumulates in chromatin in response to DNA interstrand crosslinks (ICLs), where it coordinates DNA repair through mechanisms that are still poorly understood. Here, we report that CtIP protein directly interacts with FANCD2. A region spanning amino acids 166 to 273 of CtIP and monoubiquitination of FANCD2 are both essential for the FANCD2-CtIP interaction and mitomycin C (MMC)-induced CtIP foci. Remarkably, both FANCD2 and CtIP are critical for MMC-induced RPA2 hyperphosphorylation, an event that accompanies end resection of double-strand breaks. Collectively, our results reveal a role of monoubiquitinated FANCD2 in end resection that depends on its binding to CtIP during ICL repair.
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  Data: http://www.sciencedirect.com/science/article/pii/S2211124714002927; https://doaj.org/toc/2211-1247
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  Data: 10.1016/j.celrep.2014.04.005
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