Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress.

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Standard

Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress. / Wilson, MD; Harreman, M; Taschner, M; Reid, J; Walker, J; Erdjument-Bromage, H; Tempst, P; Svejstrup, JQ.

I: Cell, Bind 154, Nr. 5, 2013, s. 983-995.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Wilson, MD, Harreman, M, Taschner, M, Reid, J, Walker, J, Erdjument-Bromage, H, Tempst, P & Svejstrup, JQ 2013, 'Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress.', Cell, bind 154, nr. 5, s. 983-995. https://doi.org/10.1016/j.cell.2013.07.028

APA

Wilson, MD., Harreman, M., Taschner, M., Reid, J., Walker, J., Erdjument-Bromage, H., Tempst, P., & Svejstrup, JQ. (2013). Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress. Cell, 154(5), 983-995. https://doi.org/10.1016/j.cell.2013.07.028

Vancouver

Wilson MD, Harreman M, Taschner M, Reid J, Walker J, Erdjument-Bromage H o.a. Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress. Cell. 2013;154(5):983-995. https://doi.org/10.1016/j.cell.2013.07.028

Author

Wilson, MD ; Harreman, M ; Taschner, M ; Reid, J ; Walker, J ; Erdjument-Bromage, H ; Tempst, P ; Svejstrup, JQ. / Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress. I: Cell. 2013 ; Bind 154, Nr. 5. s. 983-995.

Bibtex

@article{93cfd53efa054358986cc23ae72713d6,
title = "Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress.",
abstract = "DNA damage triggers polyubiquitylation and degradation of the largest subunit of RNA polymerase II (RNAPII), a “mechanism of last resort” employed during transcription stress. In yeast, this process is dependent on Def1 through a previously unresolved mechanism. Here, we report that Def1 becomes activated through ubiquitylation- and proteasome-dependent processing. Def1 processing results in the removal of a domain promoting cytoplasmic localization, resulting in nuclear accumulation of the clipped protein. Nuclear Def1 then binds RNAPII, utilizing a ubiquitin-binding domain to recruit the Elongin-Cullin E3 ligase complex via a ubiquitin-homology domain in the Ela1 protein. This facilitates polyubiquitylation of Rpb1, triggering its proteasome-mediated degradation. Together, these results outline the multistep mechanism of Rpb1 polyubiquitylation triggered by transcription stress and uncover the key role played by Def1 as a facilitator of Elongin-Cullin ubiquitin ligase function.",
author = "MD Wilson and M Harreman and M Taschner and J Reid and J Walker and H Erdjument-Bromage and P Tempst and JQ Svejstrup",
year = "2013",
doi = "10.1016/j.cell.2013.07.028",
language = "English",
volume = "154",
pages = "983--995",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "5",

}

RIS

TY - JOUR

T1 - Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress.

AU - Wilson, MD

AU - Harreman, M

AU - Taschner, M

AU - Reid, J

AU - Walker, J

AU - Erdjument-Bromage, H

AU - Tempst, P

AU - Svejstrup, JQ

PY - 2013

Y1 - 2013

N2 - DNA damage triggers polyubiquitylation and degradation of the largest subunit of RNA polymerase II (RNAPII), a “mechanism of last resort” employed during transcription stress. In yeast, this process is dependent on Def1 through a previously unresolved mechanism. Here, we report that Def1 becomes activated through ubiquitylation- and proteasome-dependent processing. Def1 processing results in the removal of a domain promoting cytoplasmic localization, resulting in nuclear accumulation of the clipped protein. Nuclear Def1 then binds RNAPII, utilizing a ubiquitin-binding domain to recruit the Elongin-Cullin E3 ligase complex via a ubiquitin-homology domain in the Ela1 protein. This facilitates polyubiquitylation of Rpb1, triggering its proteasome-mediated degradation. Together, these results outline the multistep mechanism of Rpb1 polyubiquitylation triggered by transcription stress and uncover the key role played by Def1 as a facilitator of Elongin-Cullin ubiquitin ligase function.

AB - DNA damage triggers polyubiquitylation and degradation of the largest subunit of RNA polymerase II (RNAPII), a “mechanism of last resort” employed during transcription stress. In yeast, this process is dependent on Def1 through a previously unresolved mechanism. Here, we report that Def1 becomes activated through ubiquitylation- and proteasome-dependent processing. Def1 processing results in the removal of a domain promoting cytoplasmic localization, resulting in nuclear accumulation of the clipped protein. Nuclear Def1 then binds RNAPII, utilizing a ubiquitin-binding domain to recruit the Elongin-Cullin E3 ligase complex via a ubiquitin-homology domain in the Ela1 protein. This facilitates polyubiquitylation of Rpb1, triggering its proteasome-mediated degradation. Together, these results outline the multistep mechanism of Rpb1 polyubiquitylation triggered by transcription stress and uncover the key role played by Def1 as a facilitator of Elongin-Cullin ubiquitin ligase function.

U2 - 10.1016/j.cell.2013.07.028

DO - 10.1016/j.cell.2013.07.028

M3 - Journal article

C2 - 23993092

VL - 154

SP - 983

EP - 995

JO - Cell

JF - Cell

SN - 0092-8674

IS - 5

ER -

ID: 331083929