Mitotic Histone H3 Phosphorylation by Vaccinia-Related Kinase 1 in Mammalian Cells

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Published inMolecular and Cellular Biology Vol. 27; no. 24; pp. 8533 - 8546
Main Authors Kang, Tae-Hong, Park, Do-Young, Choi, Yoon Ha, Kim, Kyung-Jin, Yoon, Ho Sup, Kim, Kyong-Tai
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.12.2007
Taylor & Francis
American Society for Microbiology (ASM)
Subjects
Animals
Cell Cycle
Cell Nucleus - enzymology
Chromatin - metabolism
Enzyme Activation
Gene Expression
HeLa Cells
Histones - metabolism
Humans
Mammals - metabolism
Mice
Mitosis
Phosphorylation
Phosphoserine - metabolism
Phosphothreonine - metabolism
Protein Binding
Protein Transport
Protein-Serine-Threonine Kinases - metabolism
Rats
Online AccessGet full text

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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList Mitotic chromatin condensation is essential for cell division in eukaryotes. Posttranslational modification of the N-terminal tail of histone proteins, particularly by phosphorylation by mitotic histone kinases, may facilitate this process. In mammals, aurora B is believed to be the mitotic histone H3 Ser10 kinase; however, it is not sufficient to phosphorylate H3 Ser10 with aurora B alone. We show that histone H3 is phosphorylated by vaccinia-related kinase 1 (VRK1). Direct phosphorylation of Thr3 and Ser10 in H3 by VRK1 both in vitro and in vivo was observed. Loss of VRK1 activity was associated with a marked decrease in H3 phosphorylation during mitosis. Phosphorylation of Ser10 by VRK1 is similar to that by aurora B. Moreover, expression and chromatin localization of VRK1 depended on the cell cycle phase. Overexpression of VRK1 resulted in a dramatic condensation of nuclei. Our findings collectively support a role of VRK1 as a novel mitotic histone H3 kinase in mammals.
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
Author Yoon Ha Choi
Kyong-Tai Kim
Tae-Hong Kang
Kyung-Jin Kim
Do-Young Park
Ho Sup Yoon
AuthorAffiliation Department of Life Science, Division of Molecular & Life Science, Pohang University of Science and Technology (POSTECH), San-31, Hyoja-Dong, Pohang 790-784, Republic of Korea, 1 X-Ray Research Group, Pohang Accelerator Laboratory, Pohang 790-784, Republic of Korea, 2 Division of Structural and Computational Biology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore 3
AuthorAffiliation_xml – name: Department of Life Science, Division of Molecular & Life Science, Pohang University of Science and Technology (POSTECH), San-31, Hyoja-Dong, Pohang 790-784, Republic of Korea, 1 X-Ray Research Group, Pohang Accelerator Laboratory, Pohang 790-784, Republic of Korea, 2 Division of Structural and Computational Biology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore 3
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  surname: Kang
  fullname: Kang, Tae-Hong
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  organization: Department of Life Science, Division of Molecular & Life Science, Pohang University of Science and Technology (POSTECH)
BackLink https://www.ncbi.nlm.nih.gov/pubmed/17938195$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: Department of Life Science, Division of Molecular & Life Science, Pohang University of Science and Technology (POSTECH), San-31, Hyoja-Dong, Pohang 790-784, Republic of Korea. Phone: 82 54 279 2297. Fax: 82 54 279 2199. E-mail: ktk@postech.ac.kr
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Mitotic chromatin condensation is essential for cell division in eukaryotes. Posttranslational modification of the N-terminal tail of histone proteins,...
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StartPage 8533
SubjectTerms Animals
Cell Cycle
Cell Nucleus - enzymology
Chromatin - metabolism
Enzyme Activation
Gene Expression
HeLa Cells
Histones - metabolism
Humans
Mammals - metabolism
Mice
Mitosis
Phosphorylation
Phosphoserine - metabolism
Phosphothreonine - metabolism
Protein Binding
Protein Transport
Protein-Serine-Threonine Kinases - metabolism
Rats
Title Mitotic Histone H3 Phosphorylation by Vaccinia-Related Kinase 1 in Mammalian Cells
URI http://mcb.asm.org/content/27/24/8533.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.00018-07
https://www.ncbi.nlm.nih.gov/pubmed/17938195
https://search.proquest.com/docview/20753916
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https://pubmed.ncbi.nlm.nih.gov/PMC2169395
Volume 27
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