Cargando…
An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth
The DNA damage checkpoint kinase Rad53 is important for the survival of budding yeast under genotoxic stresses. We performed a biochemical screen to identify proteins with specific affinity for the two Forkhead associated (FHA) domains of Rad53. The N-terminal FHA1 domain was found to coordinate a c...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2006
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064674/ https://www.ncbi.nlm.nih.gov/pubmed/17130285 http://dx.doi.org/10.1083/jcb.200605081 |
_version_ | 1782137592616058880 |
---|---|
author | Smolka, Marcus B. Chen, Sheng-hong Maddox, Paul S. Enserink, Jorrit M. Albuquerque, Claudio P. Wei, Xiao X. Desai, Arshad Kolodner, Richard D. Zhou, Huilin |
author_facet | Smolka, Marcus B. Chen, Sheng-hong Maddox, Paul S. Enserink, Jorrit M. Albuquerque, Claudio P. Wei, Xiao X. Desai, Arshad Kolodner, Richard D. Zhou, Huilin |
author_sort | Smolka, Marcus B. |
collection | PubMed |
description | The DNA damage checkpoint kinase Rad53 is important for the survival of budding yeast under genotoxic stresses. We performed a biochemical screen to identify proteins with specific affinity for the two Forkhead associated (FHA) domains of Rad53. The N-terminal FHA1 domain was found to coordinate a complex protein interaction network, which includes nuclear proteins involved in DNA damage checkpoints and transcriptional regulation. Unexpectedly, cytosolic proteins involved in cytokinesis, including septins, were also found as FHA1 binding proteins. Consistent with this interaction, a Rad53 mutant defective in its nuclear localization was found to localize to the bud neck. Abnormal morphology was observed in cells overexpressing the FHA1 domain and in rad53Δ cells under DNA replication stress. Further, septin Shs1 appears to have an important role in the response to DNA replication stress. Collectively, the results suggest a novel function of Rad53 in the regulation of polarized cell growth in response to DNA replication stress. |
format | Text |
id | pubmed-2064674 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-20646742007-11-29 An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth Smolka, Marcus B. Chen, Sheng-hong Maddox, Paul S. Enserink, Jorrit M. Albuquerque, Claudio P. Wei, Xiao X. Desai, Arshad Kolodner, Richard D. Zhou, Huilin J Cell Biol Research Articles The DNA damage checkpoint kinase Rad53 is important for the survival of budding yeast under genotoxic stresses. We performed a biochemical screen to identify proteins with specific affinity for the two Forkhead associated (FHA) domains of Rad53. The N-terminal FHA1 domain was found to coordinate a complex protein interaction network, which includes nuclear proteins involved in DNA damage checkpoints and transcriptional regulation. Unexpectedly, cytosolic proteins involved in cytokinesis, including septins, were also found as FHA1 binding proteins. Consistent with this interaction, a Rad53 mutant defective in its nuclear localization was found to localize to the bud neck. Abnormal morphology was observed in cells overexpressing the FHA1 domain and in rad53Δ cells under DNA replication stress. Further, septin Shs1 appears to have an important role in the response to DNA replication stress. Collectively, the results suggest a novel function of Rad53 in the regulation of polarized cell growth in response to DNA replication stress. The Rockefeller University Press 2006-12-04 /pmc/articles/PMC2064674/ /pubmed/17130285 http://dx.doi.org/10.1083/jcb.200605081 Text en Copyright © 2006, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Smolka, Marcus B. Chen, Sheng-hong Maddox, Paul S. Enserink, Jorrit M. Albuquerque, Claudio P. Wei, Xiao X. Desai, Arshad Kolodner, Richard D. Zhou, Huilin An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth |
title | An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth |
title_full | An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth |
title_fullStr | An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth |
title_full_unstemmed | An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth |
title_short | An FHA domain–mediated protein interaction network of Rad53 reveals its role in polarized cell growth |
title_sort | fha domain–mediated protein interaction network of rad53 reveals its role in polarized cell growth |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064674/ https://www.ncbi.nlm.nih.gov/pubmed/17130285 http://dx.doi.org/10.1083/jcb.200605081 |
work_keys_str_mv | AT smolkamarcusb anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT chenshenghong anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT maddoxpauls anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT enserinkjorritm anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT albuquerqueclaudiop anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT weixiaox anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT desaiarshad anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT kolodnerrichardd anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT zhouhuilin anfhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT smolkamarcusb fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT chenshenghong fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT maddoxpauls fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT enserinkjorritm fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT albuquerqueclaudiop fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT weixiaox fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT desaiarshad fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT kolodnerrichardd fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth AT zhouhuilin fhadomainmediatedproteininteractionnetworkofrad53revealsitsroleinpolarizedcellgrowth |