Nature Genetics
37, 931 - 933 (2005)
Published online: 21 August 2005; | doi:10.1038/ng1624
There is an Addendum (November 2005) associated with this Brief Communication.
The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemiaOrna Levran1, Claire Attwooll2, Rashida T Henry1, Kelly L Milton1, Kornelia Neveling3, Paula Rio4, 6, Sat Dev Batish1, Reinhard Kalb3, Eunike Velleuer4, Sandra Barral5, Jurg Ott5, John Petrini2, Detlev Schindler3, 7, Helmut Hanenberg4, 7
& Arleen D Auerbach1, 71
Laboratory for Human Genetics & Hematology, The Rockefeller University, New York, New York, USA. 2
Memorial Sloan-Kettering Cancer Center, New York, New York, USA. 3
Institute of Human Genetics, University of Wuerzburg, Germany. 4
Department of Pediatric Oncology, Hematology and Immunology, Children's Hospital, Heinrich Heine University, Duesseldorf, Germany. 5
Laboratory of Statistical Genetics, The Rockefeller University, New York, New York, USA. 6
Present address: CIEMAT/Marcelino Botin Foundation, Madrid, Spain. 7
These authors contributed equally to this work.
Correspondence should be addressed to Arleen D Auerbach auerbac@rockefeller.edu Seven Fanconi anemia−associated proteins (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG and FANCL) form a nuclear Fanconi anemia core complex that activates the monoubiquitination of FANCD2, targeting FANCD2 to BRCA1-containing nuclear foci. Cells from individuals with Fanconi anemia of complementation groups D1 and J (FA-D1 and FA-J) have normal FANCD2 ubiquitination. Using genetic mapping, mutation identification and western-blot data, we identify the defective protein in FA-J cells as BRIP1 (also called BACH1), a DNA helicase that is a binding partner of the breast cancer tumor suppressor BRCA1.
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