Document Detail

Replacement of charged and polar residues in the coiled-coiled interface of huntingtin-interacting protein 1 (HIP1) causes aggregation and cell death.
MedLine Citation:
PMID:  22835334     Owner:  NLM     Status:  Publisher    
HIP1 crystal structures solved in our laboratory revealed abnormalities in the coiled-coil region, suggesting intrinsic plasticity. To test this, specific amino acids in the coiled-coil were mutated. The apparent thermal stability of HIP1 was altered when Thr528 and Glu531 were replaced by leucine, and was enhanced when Lys510 was also mutated. In cells, HIP1 mutant expression produced aggregation. MTS and flow cytometry indicate a correlation between aggregated HIP1 and enhanced cell death. These data support the idea that flexibility of the HIP1 coiled-coil domain is important for normal function and may lead to new insights into Huntington's disease.
S N Fontaine; S P Bauer; X Lin; S Poorfarhani; J A Ybe
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-7-23
Journal Detail:
Title:  FEBS letters     Volume:  -     ISSN:  1873-3468     ISO Abbreviation:  -     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-7-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier B.V.
Department of Molecular and Cellular Biochemistry, Indiana University Bloomington, 212 S. Hawthorne Drive, Bloomington, IN 47405.
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