RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites

Bijan Sobhian; Genze Shao; Dana R. Lilli; Aedin C. Culhane; Lisa A. Moreau; Bing Xia; David M. Livingston; Roger A. Greenberg

doi:10.1126/science.1139516

RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites

Bijan Sobhian
, Genze Shao
, Dana R. Lilli
, Aedin C. Culhane
, Lisa A. Moreau
, Bing Xia
, David M. Livingston
, Roger A. Greenberg

Research output: Contribution to journal › Article › peer-review

Abstract

Mutations affecting the BRCT domains of the breast cancer -associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs). The molecular structures at DSBs recognized by BRCA1 are presently unknown. We report the interaction of the BRCA1 BRCT domain with RAP80, a ubiquitin-binding protein. RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-γH2AX-dependent lysine ⁶- and lysine⁶³-linked ubiquitin polymers at DSBs. These events are required for cell cycle checkpoint and repair responses to ionizing radiation, implicating ubiquitin chain recognition and turnover in the BRCA1-mediated repair of DSBs.

Original language	English
Pages (from-to)	1198-1202
Number of pages	5
Journal	Science
Volume	316
Issue number	5828
DOIs	https://doi.org/10.1126/science.1139516
Publication status	Published - 25 May 2007
Externally published	Yes

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title = "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites",

abstract = "Mutations affecting the BRCT domains of the breast cancer -associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs). The molecular structures at DSBs recognized by BRCA1 are presently unknown. We report the interaction of the BRCA1 BRCT domain with RAP80, a ubiquitin-binding protein. RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-γH2AX-dependent lysine 6- and lysine63-linked ubiquitin polymers at DSBs. These events are required for cell cycle checkpoint and repair responses to ionizing radiation, implicating ubiquitin chain recognition and turnover in the BRCA1-mediated repair of DSBs.",

author = "Bijan Sobhian and Genze Shao and Lilli, \{Dana R.\} and Culhane, \{Aedin C.\} and Moreau, \{Lisa A.\} and Bing Xia and Livingston, \{David M.\} and Greenberg, \{Roger A.\}",

year = "2007",

month = may,

day = "25",

doi = "10.1126/science.1139516",

language = "English",

volume = "316",

pages = "1198--1202",

journal = "Science",

issn = "0036-8075",

number = "5828",

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TY - JOUR

T1 - RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites

AU - Sobhian, Bijan

AU - Shao, Genze

AU - Lilli, Dana R.

AU - Culhane, Aedin C.

AU - Moreau, Lisa A.

AU - Xia, Bing

AU - Livingston, David M.

AU - Greenberg, Roger A.

PY - 2007/5/25

Y1 - 2007/5/25

N2 - Mutations affecting the BRCT domains of the breast cancer -associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs). The molecular structures at DSBs recognized by BRCA1 are presently unknown. We report the interaction of the BRCA1 BRCT domain with RAP80, a ubiquitin-binding protein. RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-γH2AX-dependent lysine 6- and lysine63-linked ubiquitin polymers at DSBs. These events are required for cell cycle checkpoint and repair responses to ionizing radiation, implicating ubiquitin chain recognition and turnover in the BRCA1-mediated repair of DSBs.

AB - Mutations affecting the BRCT domains of the breast cancer -associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs). The molecular structures at DSBs recognized by BRCA1 are presently unknown. We report the interaction of the BRCA1 BRCT domain with RAP80, a ubiquitin-binding protein. RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-γH2AX-dependent lysine 6- and lysine63-linked ubiquitin polymers at DSBs. These events are required for cell cycle checkpoint and repair responses to ionizing radiation, implicating ubiquitin chain recognition and turnover in the BRCA1-mediated repair of DSBs.

UR - https://www.scopus.com/pages/publications/34249949779

U2 - 10.1126/science.1139516

DO - 10.1126/science.1139516

M3 - Article

C2 - 17525341

AN - SCOPUS:34249949779

SN - 0036-8075

VL - 316

SP - 1198

EP - 1202

JO - Science

JF - Science

IS - 5828

ER -

RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites

Abstract

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