Fumiko Esashi

Profile
2001-2007  Cancer Research UK London Research Institute Postdoc
2007-2013 Oxford University CRUK CDA fellow
2011-2015 Oxford University Research Lecturer
2013- Oxford University Wellcome Trust SRA
2015- Oxford University Associate Professor

Field of Specialization
Genome stability / DNA repair / Cell cycle / Molecular cellular biology / Biochemistry

Oxford University(U.K.)

 https://esashilab.wordpress.com/
fumiko.esashi@path.ox.ac.uk

Research Hub Group :Cutting-edge Cell Biology international hub group

Research Highlights

  • Dr Esashi aims to understand how proliferating human cells guard their genomic DNA against various stresses coming from the environment and from normal processes of cell growth. Her previous studies revealed several unexpected regulatory mechanisms, whereby the key DNA repair proteins Rad51, BRCA2 and PALB2 are regulated by central cell cycle kinases such as cyclin-dependent kinases (CDKs) and polo-like kinase 1 (Plk1) in proliferating human cells. The group continues to tackle challenging questions regarding the regulation of DNA repair using a multidisciplinary approach, including protein biochemistry, molecular and cellular biology, bioimaging, bioinformatics and mathematical modelling.

Selected Awards

  • 2015-
    Associate Professor (University of Oxford)
  • 2013-
    Wellcome Trust Senior Research Fellowship Award
  • 2011-2015
    University Research Lecturer (University of Oxford)
  • 2007-2013
    Cancer Research UK Career Development Award

Selected Publications 

  • Yata K, Bleuyard JY, Nakato R, Ralf C, Kato Y, Schwab RA, Niedzwiedz W, Shirahige K, Esashi F (2014) BRCA2 coordinates the activities of cell-cycle kinases to promote genome stability. Cell Rep. 7, 1547-59
  • Bleuyard JY, Buisson R, Masson JY, Esashi F (2012) ChAM, a novel motif that mediates PALB2 intrinsic chromatin binding and facilitates DNA repair. EMBO Rep. 13, 135-41
  • Yata K, Lloyd J, Maslen S, Bleuyard JY, Skehel M, Smerdon S., Esashi F (2012) Plk1 and CK2 act in concert to regulate Rad51 during DNA double strand break repair. Mol. Cell 45, 371-83
  • Esashi F, Galkin VE, Yu X, Egelman E, West SC (2007) Stabilisation of RAD51 nucleoprotein filament by the C-terminal region of BRCA2. Nat Struc Mol Biol. 14, 468-474
  • Esashi F, Christ N, Gannon J, Liu Y, Hunt T, Jasin M, West SC (2005) CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair. Nature (Article), 434, 598-604