Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure

The multi-subunit Anaphase Promoting Complex (APC) is an essential cell cycle regulator. Although CDC26 is known to play a role in APC assembly, its molecular function has remained unclear. Biophysical, structural, and genetic studies presented here reveal that CDC26 stabilizes the structure of APC6...

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Autores principales: Wang, Jing, Dye, Billy T., Rajashankar, Kanagalaghatta R., Kurinov, Igor, Schulman, Brenda A.
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2759704/
https://www.ncbi.nlm.nih.gov/pubmed/19668213
http://dx.doi.org/10.1038/nsmb.1645
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author Wang, Jing
Dye, Billy T.
Rajashankar, Kanagalaghatta R.
Kurinov, Igor
Schulman, Brenda A.
author_facet Wang, Jing
Dye, Billy T.
Rajashankar, Kanagalaghatta R.
Kurinov, Igor
Schulman, Brenda A.
author_sort Wang, Jing
collection PubMed
description The multi-subunit Anaphase Promoting Complex (APC) is an essential cell cycle regulator. Although CDC26 is known to play a role in APC assembly, its molecular function has remained unclear. Biophysical, structural, and genetic studies presented here reveal that CDC26 stabilizes the structure of APC6, a core TPR protein required for APC integrity. Interestingly, CDC26–APC6 association involves an intermolecular TPR mimic composed of one helix from each protein.
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spelling pubmed-27597042010-03-01 Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure Wang, Jing Dye, Billy T. Rajashankar, Kanagalaghatta R. Kurinov, Igor Schulman, Brenda A. Nat Struct Mol Biol Article The multi-subunit Anaphase Promoting Complex (APC) is an essential cell cycle regulator. Although CDC26 is known to play a role in APC assembly, its molecular function has remained unclear. Biophysical, structural, and genetic studies presented here reveal that CDC26 stabilizes the structure of APC6, a core TPR protein required for APC integrity. Interestingly, CDC26–APC6 association involves an intermolecular TPR mimic composed of one helix from each protein. 2009-08-09 2009-09 /pmc/articles/PMC2759704/ /pubmed/19668213 http://dx.doi.org/10.1038/nsmb.1645 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Wang, Jing
Dye, Billy T.
Rajashankar, Kanagalaghatta R.
Kurinov, Igor
Schulman, Brenda A.
Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure
title Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure
title_full Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure
title_fullStr Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure
title_full_unstemmed Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure
title_short Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26–APC6 structure
title_sort insights into anaphase promoting complex tpr subdomain assembly from a cdc26–apc6 structure
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2759704/
https://www.ncbi.nlm.nih.gov/pubmed/19668213
http://dx.doi.org/10.1038/nsmb.1645
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