Chk1 and Claspin potentiate PCNA ubiquitination

Chk1 is a kinase crucial for genomic integrity and an effector of ATR (ATM and Rad3-related) in DNA damage response. Here, we show that Chk1 regulates the DNA damage-induced ubiquitination of proliferating cell nuclear antigen (PCNA), which facilitates the continuous replication of damaged DNA. Surp...

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Published inGenes & development Vol. 22; no. 9; pp. 1147 - 1152
Main Authors Yang, Xiaohong H, Shiotani, Bunsyo, Classon, Marie, Zou, Lee
Format Journal Article
LanguageEnglish
Published United States Cold Spring Harbor Laboratory Press 01.05.2008
Subjects
Adaptor Proteins, Signal Transducing - genetics
Adaptor Proteins, Signal Transducing - metabolism
Ataxia Telangiectasia Mutated Proteins
Blotting, Western
Cell Cycle Proteins - antagonists & inhibitors
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Cell Line, Tumor
Checkpoint Kinase 1
DNA Replication - genetics
HeLa Cells
Humans
Hydroxyurea - pharmacology
Morpholines - pharmacology
Plasmids - genetics
Proliferating Cell Nuclear Antigen - metabolism
Protein Kinases - genetics
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases - antagonists & inhibitors
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Pyrones - pharmacology
Research Communication
RNA, Small Interfering - genetics
Transfection
Ubiquitination - drug effects
Ubiquitination - radiation effects
Ultraviolet Rays
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Abstract Chk1 is a kinase crucial for genomic integrity and an effector of ATR (ATM and Rad3-related) in DNA damage response. Here, we show that Chk1 regulates the DNA damage-induced ubiquitination of proliferating cell nuclear antigen (PCNA), which facilitates the continuous replication of damaged DNA. Surprisingly, this Chk1 function requires the DNA replication protein Claspin but not ATR. Claspin, which is stabilized by Chk1, regulates the binding of the ubiquitin ligase Rad18 to chromatin. Timeless, a Claspin-associating protein, is also required for efficient PCNA ubiquitination. Thus, Chk1 and the Claspin-Timeless module of replication forks not only participate in ATR signaling, but also protect stressed forks independently of ATR.
AbstractList Chk1 is a kinase crucial for genomic integrity and an effector of ATR (ATM and Rad3-realated) in DNA damage response. Here, we show that Chk1 regulates the DNA damage-induced ubiquitination of proliferating cell nuclear antigen (PCNA), which facilitates the continuous replication of damaged DNA. Surprisingly, this Chk1 function requires the DNA replication protein Claspin but not ATR. Claspin, which is stabilized by Chk1, regulates the binding of the ubiquitin ligase Rad18 to chromatin. Timeless, a Claspin-associating protein, is also required for efficient PCNA ubiquitination. Thus, Chk1 and the Claspin–Timeless module of replication forks not only participate in ATR signaling, but also protect stressed forks independently of ATR.
Chk1 is a kinase crucial for genomic integrity and an effector of ATR (ATM and Rad3-related) in DNA damage response. Here, we show that Chk1 regulates the DNA damage-induced ubiquitination of proliferating cell nuclear antigen (PCNA), which facilitates the continuous replication of damaged DNA. Surprisingly, this Chk1 function requires the DNA replication protein Claspin but not ATR. Claspin, which is stabilized by Chk1, regulates the binding of the ubiquitin ligase Rad18 to chromatin. Timeless, a Claspin-associating protein, is also required for efficient PCNA ubiquitination. Thus, Chk1 and the Claspin-Timeless module of replication forks not only participate in ATR signaling, but also protect stressed forks independently of ATR.
Author Zou, Lee
Yang, Xiaohong H
Shiotani, Bunsyo
Classon, Marie
AuthorAffiliation 1 Massachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, Massachusetts 02129, USA
2 Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA
AuthorAffiliation_xml – name: 1 Massachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, Massachusetts 02129, USA
– name: 2 Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA
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  givenname: Xiaohong H
  surname: Yang
  fullname: Yang, Xiaohong H
  organization: Massachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, Massachusetts 02129, USA
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  givenname: Bunsyo
  surname: Shiotani
  fullname: Shiotani, Bunsyo
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  givenname: Marie
  surname: Classon
  fullname: Classon, Marie
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  givenname: Lee
  surname: Zou
  fullname: Zou, Lee
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Snippet Chk1 is a kinase crucial for genomic integrity and an effector of ATR (ATM and Rad3-related) in DNA damage response. Here, we show that Chk1 regulates the DNA...
Chk1 is a kinase crucial for genomic integrity and an effector of ATR (ATM and Rad3-realated) in DNA damage response. Here, we show that Chk1 regulates the DNA...
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SubjectTerms Adaptor Proteins, Signal Transducing - genetics
Adaptor Proteins, Signal Transducing - metabolism
Ataxia Telangiectasia Mutated Proteins
Blotting, Western
Cell Cycle Proteins - antagonists & inhibitors
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Cell Line, Tumor
Checkpoint Kinase 1
DNA Replication - genetics
HeLa Cells
Humans
Hydroxyurea - pharmacology
Morpholines - pharmacology
Plasmids - genetics
Proliferating Cell Nuclear Antigen - metabolism
Protein Kinases - genetics
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases - antagonists & inhibitors
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Pyrones - pharmacology
Research Communication
RNA, Small Interfering - genetics
Transfection
Ubiquitination - drug effects
Ubiquitination - radiation effects
Ultraviolet Rays
Title Chk1 and Claspin potentiate PCNA ubiquitination
URI https://www.ncbi.nlm.nih.gov/pubmed/18451105
https://search.proquest.com/docview/19800468
https://pubmed.ncbi.nlm.nih.gov/PMC2335311
Volume 22
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