The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage

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Standard

The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. / Stewart, Grant S.; Panier, Stephanie; Townsend, Kelly; Al-Hakim, Abdallah K.; Kolas, Nadine K.; Miller, Edward S.; Nakada, Shinichiro; Ylanko, Jarkko; Olivarius, Signe; Mendez, Megan; Oldreive, Ceri; Wildenhain, Jan; Tagliaferro, Andrea; Pelletier, Laurence; Taubenheim, Nadine; Durandy, Anne; Byrd, Philip J.; Stankovic, Tatjana; Taylor, A. Malcolm R.; Durocher, Daniel.

I: Cell, Bind 136, Nr. 3, 2009, s. 420-434.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Stewart, GS, Panier, S, Townsend, K, Al-Hakim, AK, Kolas, NK, Miller, ES, Nakada, S, Ylanko, J, Olivarius, S, Mendez, M, Oldreive, C, Wildenhain, J, Tagliaferro, A, Pelletier, L, Taubenheim, N, Durandy, A, Byrd, PJ, Stankovic, T, Taylor, AMR & Durocher, D 2009, 'The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage', Cell, bind 136, nr. 3, s. 420-434. https://doi.org/10.1016/j.cell.2008.12.042

APA

Stewart, G. S., Panier, S., Townsend, K., Al-Hakim, A. K., Kolas, N. K., Miller, E. S., Nakada, S., Ylanko, J., Olivarius, S., Mendez, M., Oldreive, C., Wildenhain, J., Tagliaferro, A., Pelletier, L., Taubenheim, N., Durandy, A., Byrd, P. J., Stankovic, T., Taylor, A. M. R., & Durocher, D. (2009). The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell, 136(3), 420-434. https://doi.org/10.1016/j.cell.2008.12.042

Vancouver

Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, Miller ES o.a. The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell. 2009;136(3):420-434. https://doi.org/10.1016/j.cell.2008.12.042

Author

Stewart, Grant S. ; Panier, Stephanie ; Townsend, Kelly ; Al-Hakim, Abdallah K. ; Kolas, Nadine K. ; Miller, Edward S. ; Nakada, Shinichiro ; Ylanko, Jarkko ; Olivarius, Signe ; Mendez, Megan ; Oldreive, Ceri ; Wildenhain, Jan ; Tagliaferro, Andrea ; Pelletier, Laurence ; Taubenheim, Nadine ; Durandy, Anne ; Byrd, Philip J. ; Stankovic, Tatjana ; Taylor, A. Malcolm R. ; Durocher, Daniel. / The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. I: Cell. 2009 ; Bind 136, Nr. 3. s. 420-434.

Bibtex

@article{e73462701a7511df8ed1000ea68e967b,
title = "The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage",
abstract = "The biological response to DNA double-strand breaks acts to preserve genome integrity. Individuals bearing inactivating mutations in components of this response exhibit clinical symptoms that include cellular radiosensitivity, immunodeficiency, and cancer predisposition. The archetype for such disorders is Ataxia-Telangiectasia caused by biallelic mutation in ATM, a central component of the DNA damage response. Here, we report that the ubiquitin ligase RNF168 is mutated in the RIDDLE syndrome, a recently discovered immunodeficiency and radiosensitivity disorder. We show that RNF168 is recruited to sites of DNA damage by binding to ubiquitylated histone H2A. RNF168 acts with UBC13 to amplify the RNF8-dependent histone ubiquitylation by targeting H2A-type histones and by promoting the formation of lysine 63-linked ubiquitin conjugates. These RNF168-dependent chromatin modifications orchestrate the accumulation of 53BP1 and BRCA1 to DNA lesions, and their loss is the likely cause of the cellular and developmental phenotypes associated with RIDDLE syndrome.",
keywords = "Faculty of Science, DNA, signalering, DNA, signaling",
author = "Stewart, {Grant S.} and Stephanie Panier and Kelly Townsend and Al-Hakim, {Abdallah K.} and Kolas, {Nadine K.} and Miller, {Edward S.} and Shinichiro Nakada and Jarkko Ylanko and Signe Olivarius and Megan Mendez and Ceri Oldreive and Jan Wildenhain and Andrea Tagliaferro and Laurence Pelletier and Nadine Taubenheim and Anne Durandy and Byrd, {Philip J.} and Tatjana Stankovic and Taylor, {A. Malcolm R.} and Daniel Durocher",
note = "Paper id:: 19203578",
year = "2009",
doi = "10.1016/j.cell.2008.12.042",
language = "English",
volume = "136",
pages = "420--434",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage

AU - Stewart, Grant S.

AU - Panier, Stephanie

AU - Townsend, Kelly

AU - Al-Hakim, Abdallah K.

AU - Kolas, Nadine K.

AU - Miller, Edward S.

AU - Nakada, Shinichiro

AU - Ylanko, Jarkko

AU - Olivarius, Signe

AU - Mendez, Megan

AU - Oldreive, Ceri

AU - Wildenhain, Jan

AU - Tagliaferro, Andrea

AU - Pelletier, Laurence

AU - Taubenheim, Nadine

AU - Durandy, Anne

AU - Byrd, Philip J.

AU - Stankovic, Tatjana

AU - Taylor, A. Malcolm R.

AU - Durocher, Daniel

N1 - Paper id:: 19203578

PY - 2009

Y1 - 2009

N2 - The biological response to DNA double-strand breaks acts to preserve genome integrity. Individuals bearing inactivating mutations in components of this response exhibit clinical symptoms that include cellular radiosensitivity, immunodeficiency, and cancer predisposition. The archetype for such disorders is Ataxia-Telangiectasia caused by biallelic mutation in ATM, a central component of the DNA damage response. Here, we report that the ubiquitin ligase RNF168 is mutated in the RIDDLE syndrome, a recently discovered immunodeficiency and radiosensitivity disorder. We show that RNF168 is recruited to sites of DNA damage by binding to ubiquitylated histone H2A. RNF168 acts with UBC13 to amplify the RNF8-dependent histone ubiquitylation by targeting H2A-type histones and by promoting the formation of lysine 63-linked ubiquitin conjugates. These RNF168-dependent chromatin modifications orchestrate the accumulation of 53BP1 and BRCA1 to DNA lesions, and their loss is the likely cause of the cellular and developmental phenotypes associated with RIDDLE syndrome.

AB - The biological response to DNA double-strand breaks acts to preserve genome integrity. Individuals bearing inactivating mutations in components of this response exhibit clinical symptoms that include cellular radiosensitivity, immunodeficiency, and cancer predisposition. The archetype for such disorders is Ataxia-Telangiectasia caused by biallelic mutation in ATM, a central component of the DNA damage response. Here, we report that the ubiquitin ligase RNF168 is mutated in the RIDDLE syndrome, a recently discovered immunodeficiency and radiosensitivity disorder. We show that RNF168 is recruited to sites of DNA damage by binding to ubiquitylated histone H2A. RNF168 acts with UBC13 to amplify the RNF8-dependent histone ubiquitylation by targeting H2A-type histones and by promoting the formation of lysine 63-linked ubiquitin conjugates. These RNF168-dependent chromatin modifications orchestrate the accumulation of 53BP1 and BRCA1 to DNA lesions, and their loss is the likely cause of the cellular and developmental phenotypes associated with RIDDLE syndrome.

KW - Faculty of Science

KW - DNA

KW - signalering

KW - DNA

KW - signaling

U2 - 10.1016/j.cell.2008.12.042

DO - 10.1016/j.cell.2008.12.042

M3 - Journal article

C2 - 19203578

VL - 136

SP - 420

EP - 434

JO - Cell

JF - Cell

SN - 0092-8674

IS - 3

ER -

ID: 17901596