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FANCD2 binds CtIP and regulates DNA-end resection during DNA interstrand crosslink repair.

Abstract：

: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.

journal_name

Cell Rep

journal_title

Cell reports

authors

Unno J,Itaya A,Taoka M,Sato K,Tomida J,Sakai W,Sugasawa K,Ishiai M,Ikura T,Isobe T,Kurumizaka H,Takata M

doi

10.1016/j.celrep.2014.04.005

subject

Has Abstract

pub_date

2014-05-22 00:00:00

pages

1039-47

issue

4

issn

2211-1247

pii

S2211-1247(14)00292-7

journal_volume

7

pub_type

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