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CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins. / Parsons, Jason L.; Tait, Philip S.; Finch, David et al.
In: Molecular Cell, Vol. 29, No. 4, 29.02.2008, p. 477-487.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Parsons, JL, Tait, PS, Finch, D, Dianova, II, Allinson, SL & Dianov, GL 2008, 'CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins.', Molecular Cell, vol. 29, no. 4, pp. 477-487. https://doi.org/10.1016/j.molcel.2007.12.027

APA

Parsons, J. L., Tait, P. S., Finch, D., Dianova, I. I., Allinson, S. L., & Dianov, G. L. (2008). CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins. Molecular Cell, 29(4), 477-487. https://doi.org/10.1016/j.molcel.2007.12.027

Vancouver

Parsons JL, Tait PS, Finch D, Dianova II, Allinson SL, Dianov GL. CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins. Molecular Cell. 2008 Feb 29;29(4):477-487. doi: 10.1016/j.molcel.2007.12.027

Author

Parsons, Jason L. ; Tait, Philip S. ; Finch, David et al. / CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins. In: Molecular Cell. 2008 ; Vol. 29, No. 4. pp. 477-487.

Bibtex

@article{93c2c5c6cc4340d19de15128896b9f34,
title = "CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins.",
abstract = "Base excision repair (BER) is the major pathway for processing of simple lesions in DNA, including single-strand breaks, base damage, and base loss. The scaffold protein XRCC1, DNA polymerase β, and DNA ligase III play pivotal roles in BER. Although all these enzymes are essential for development, their cellular levels must be tightly regulated because increased amounts of BER enzymes lead to elevated mutagenesis and genetic instability and are frequently found in cancer cells. Here we report that BER enzyme levels are linked to and controlled by the level of DNA lesions. We demonstrate that stability of BER enzymes increases after formation of a repair complex on damaged DNA and that proteins not involved in a repair complex are ubiquitylated by the E3 ubiquitin ligase CHIP and subsequently rapidly degraded. These data identify a molecular mechanism controlling cellular levels of BER enzymes and correspondingly the efficiency and capacity of BER.",
keywords = "DNA",
author = "Parsons, {Jason L.} and Tait, {Philip S.} and David Finch and Dianova, {Irina I.} and Allinson, {Sarah L.} and Dianov, {Grigory L.}",
year = "2008",
month = feb,
day = "29",
doi = "10.1016/j.molcel.2007.12.027",
language = "English",
volume = "29",
pages = "477--487",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins.

AU - Parsons, Jason L.

AU - Tait, Philip S.

AU - Finch, David

AU - Dianova, Irina I.

AU - Allinson, Sarah L.

AU - Dianov, Grigory L.

PY - 2008/2/29

Y1 - 2008/2/29

N2 - Base excision repair (BER) is the major pathway for processing of simple lesions in DNA, including single-strand breaks, base damage, and base loss. The scaffold protein XRCC1, DNA polymerase β, and DNA ligase III play pivotal roles in BER. Although all these enzymes are essential for development, their cellular levels must be tightly regulated because increased amounts of BER enzymes lead to elevated mutagenesis and genetic instability and are frequently found in cancer cells. Here we report that BER enzyme levels are linked to and controlled by the level of DNA lesions. We demonstrate that stability of BER enzymes increases after formation of a repair complex on damaged DNA and that proteins not involved in a repair complex are ubiquitylated by the E3 ubiquitin ligase CHIP and subsequently rapidly degraded. These data identify a molecular mechanism controlling cellular levels of BER enzymes and correspondingly the efficiency and capacity of BER.

AB - Base excision repair (BER) is the major pathway for processing of simple lesions in DNA, including single-strand breaks, base damage, and base loss. The scaffold protein XRCC1, DNA polymerase β, and DNA ligase III play pivotal roles in BER. Although all these enzymes are essential for development, their cellular levels must be tightly regulated because increased amounts of BER enzymes lead to elevated mutagenesis and genetic instability and are frequently found in cancer cells. Here we report that BER enzyme levels are linked to and controlled by the level of DNA lesions. We demonstrate that stability of BER enzymes increases after formation of a repair complex on damaged DNA and that proteins not involved in a repair complex are ubiquitylated by the E3 ubiquitin ligase CHIP and subsequently rapidly degraded. These data identify a molecular mechanism controlling cellular levels of BER enzymes and correspondingly the efficiency and capacity of BER.

KW - DNA

UR - http://www.scopus.com/inward/record.url?scp=39549106043&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2007.12.027

DO - 10.1016/j.molcel.2007.12.027

M3 - Journal article

VL - 29

SP - 477

EP - 487

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

ER -