Document Detail

A 629RKLKK633 motif in the hinge region controls the androgen receptor at multiple levels.
MedLine Citation:
PMID:  20186458     Owner:  NLM     Status:  MEDLINE    
The androgen receptor protein has specific domains involved in DNA binding, ligand binding, and transactivation, whose activities need to be integrated during transcription activation. The hinge region, more particular a (629)RKLKK(633) motif, seems to play a crucial role in this process. Indeed, although the motif is not part of the DNA-binding domain, its positive residues are involved in optimal DNA binding and nuclear translocation as shown by mutation analysis. When the mutated ARs are forced into the nucleus, however, the residues seem to play different roles in transactivation. Moreover, we show by FRAP analysis that during activation, the AR is distributed in the nucleus in a mobile and two immobile fractions, and that mutations in the (629)RKLKK(633) motif affect the distribution of the AR over these three intranuclear fractions. Taken together, the (629)RKLKK(633) motif is a multifunctional motif that integrates nuclear localization, receptor stability, DNA binding, transactivation potential and intranuclear mobility.
Tamzin M Tanner; Sarah Denayer; Bart Geverts; Nora Van Tilborgh; Stefanie Kerkhofs; Christine Helsen; Lien Spans; Vanessa Dubois; Adriaan B Houtsmuller; Frank Claessens; Annemie Haelens
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-02-26
Journal Detail:
Title:  Cellular and molecular life sciences : CMLS     Volume:  67     ISSN:  1420-9071     ISO Abbreviation:  Cell. Mol. Life Sci.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-05-11     Completed Date:  2010-05-25     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9705402     Medline TA:  Cell Mol Life Sci     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  1919-27     Citation Subset:  IM    
Molecular Endocrinology Laboratory, Department of Molecular Cell Biology, Catholic University of Leuven, Campus Gasthuisberg O&N1, Herestraat 49, Box 901, 3000, Leuven, Belgium.
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MeSH Terms
Amino Acid Motifs
Amino Acid Substitution
Binding Sites
COS Cells
Cell Nucleus / metabolism
Cercopithecus aethiops
DNA / metabolism
Fluorescence Recovery After Photobleaching
Hela Cells
Mutagenesis, Site-Directed
Protein Stability
Protein Structure, Tertiary
Receptors, Androgen / chemistry*,  genetics,  metabolism*
Recombinant Fusion Proteins / chemistry,  genetics,  metabolism
Sequence Deletion
Transcriptional Activation
Reg. No./Substance:
0/AR protein, human; 0/Receptors, Androgen; 0/Recombinant Fusion Proteins; 9007-49-2/DNA

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