title: CBP-mediated post-translational N-glycosylation of BRCA2.
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.
authors: Cancer Biology Program, Department of OB/GYN, Morehouse School of Medicine, Georgia Cancer Center for Excellence, Grady Health System, Atlanta, GA 30303, USA.
authors: Habibur
authors: H
authors: Siddique
authors: Veena N
authors: VN
authors: Rao
authors: E Shyam P
authors: ES
authors: Reddy
mesh_terms: D051017:Apoptosis Regulatory Proteins; D024682:BRCA2 Protein / Q000378:metabolism*; D050882:CREB-Binding Protein / Q000737:chemistry / Q000502:physiology*; D045744:Cell Line, Tumor; D005260:Female; D006031:Glycosylation; D006801:Humans; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary
chemical_list: D051017:Apoptosis Regulatory Proteins; C118024:BLID protein, human; D024682:BRCA2 Protein; C551750:BRCA2 protein, human; D050882:CREB-Binding Protein; C494363:CREBBP protein, human