CBP-mediated post-translational N-glycosylation of BRCA2

  • Authors:
    • Habibur Siddique
    • Veena N. Rao
    • E. Shyam P. Reddy
  • Corresponding author:
  • View Affiliations

  • Published online on: Saturday, August 1, 2009
  • Pages: 387-391 DOI: 10.3892/ijo_00000351

Abstract

CREB binding protein (CBP) is a transcriptional cofactor with intrinsic histone acetyl transferase activity (HAT). We have observed that CBP interacts with BRCA2 and mediates post-translational glycosylation of BRCA2. The binding of CBP to the amino-terminal region of BRCA2 is necessary for the glycosylation at residue 272 of BRCA2. Digestion with peptide N-glycosidase F indicates that the glycosylation of BRCA2 is N-linked. It is possible that this novel CBP-mediated post-translational N-glycosylation activity alters the conformation of CBP-interacting proteins, leading to regulation of gene expression, cell growth and differentiation.
Journal Cover

August 2009
Volume 35 Issue 2

Print ISSN: 1019-6439
Online ISSN:1791-2423

2013 Impact Factor: 2.773
2014 I.F. (Expected) ≥ 3.310 Ranked #30/202 Oncology
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APA
Siddique, H., Rao, V.N., & Reddy, E.S. (2009). CBP-mediated post-translational N-glycosylation of BRCA2. International Journal of Oncology, 35, 387-391. http://dx.doi.org/10.3892/ijo_00000351
MLA
Siddique, H., Rao, V. N., Reddy, E. S."CBP-mediated post-translational N-glycosylation of BRCA2". International Journal of Oncology 35.2 (2009): 387-391.
Chicago
Siddique, H., Rao, V. N., Reddy, E. S."CBP-mediated post-translational N-glycosylation of BRCA2". International Journal of Oncology 35, no. 2 (2009): 387-391. http://dx.doi.org/10.3892/ijo_00000351