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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2009-7-6
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1019-6439
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
387-91
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:19578754-Apoptosis Regulatory Proteins,
pubmed-meshheading:19578754-BRCA2 Protein,
pubmed-meshheading:19578754-CREB-Binding Protein,
pubmed-meshheading:19578754-Cell Line, Tumor,
pubmed-meshheading:19578754-Female,
pubmed-meshheading:19578754-Glycosylation,
pubmed-meshheading:19578754-Humans,
pubmed-meshheading:19578754-Protein Processing, Post-Translational,
pubmed-meshheading:19578754-Protein Structure, Tertiary
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pubmed:year |
2009
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pubmed:articleTitle |
CBP-mediated post-translational N-glycosylation of BRCA2.
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pubmed:affiliation |
Cancer Biology Program, Department of OB/GYN, Morehouse School of Medicine, Georgia Cancer Center for Excellence, Grady Health System, Atlanta, GA 30303, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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