Document Detail


MAPK modulates the DNA binding of adipocyte enhancer-binding protein 1.
MedLine Citation:
PMID:  15654748     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Adipocyte enhancer-binding protein 1 (AEBP1) is a down-regulator of adipogenesis through its transcriptional repression activity, as well as through its interaction with mitogen-activated protein kinase (MAPK), which protects MAPK from its specific phosphatases. This study increases our understanding of the mechanisms of DNA binding by AEBP1, the first step in its function as a transcriptional repressor. We show that DNA binding by AEBP1 requires both the N- and C-terminal domains of AEBP1, and MAPK interaction with AEBP1 (through its N terminus) results in enhanced DNA binding. A threonine at position 623 within the C-terminal domain of AEBP1 plays an important role in DNA binding by AEBP1, because the mutation results in decreased DNA binding by AEBP1, which leads to a decrease in the transcriptional repression ability of AEBP1. We also show that in vitro phosphorylation of AEBP1 by MAPK is greatly reduced upon mutation of T623. These results suggest that MAPK regulates the transcriptional activity of AEBP1 by a novel dual mechanism, in which MAPK interaction enhances and subsequent phosphorylation decreases the DNA-binding ability of AEBP1.
Authors:
Peter J Lyons; Aleixo M Muise; Hyo-Sung Ro
Related Documents :
19815308 - Different gene regulation strategies revealed by analysis of binding motifs.
2910848 - Multiple protein-dna interactions within the human interferon-beta regulatory element.
1718998 - Delayed secondary glucocorticoid response elements. unusual nucleotide motifs specify g...
22547138 - Comparative study of the glycan specificities of cell-bound human tandem repeat-type ga...
1531028 - Effects of dimethyl sulfoxide on catalysis in escherichia coli f1-atpase.
6347198 - Heterotropic interactions of amp and glucose binding sites in phosphorylase a are destr...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  44     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  2005 Jan 
Date Detail:
Created Date:  2005-01-18     Completed Date:  2005-04-12     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  926-31     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Carboxypeptidases
DNA / metabolism*
Electrophoretic Mobility Shift Assay
Mice
Mitogen-Activated Protein Kinases / chemistry,  genetics,  metabolism*
Molecular Sequence Data
NIH 3T3 Cells
Phosphorylation
Protein Binding
Proteins / metabolism*
Recombinant Proteins / metabolism
Repressor Proteins
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/AEBP1 protein, human; 0/Proteins; 0/Recombinant Proteins; 0/Repressor Proteins; 9007-49-2/DNA; EC 2.7.11.24/Mitogen-Activated Protein Kinases; EC 3.4.-/Carboxypeptidases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Role of a surface tryptophan in defining the structure, stability, and DNA binding of the hypertherm...
Next Document:  Integrin-linked kinase complexes with caveolin-1 in human neuroblastoma cells.