PARP1-dependent recruitment of the FBXL10-RNF68-RNF2 ubiquitin ligase to sites of DNA damage controls H2A.Z loading
The mammalian FBXL10-RNF68-RNF2 ubiquitin ligase complex (FRRUC) mono-ubiquitylates H2A at Lys119 to repress transcription in unstressed cells. We found that the FRRUC is rapidly and transiently recruited to sites of DNA damage in a PARP1- and TIMELESS-dependent manner to promote mono-ubiquitylation...
Main Authors: | Gergely Rona, Domenico Roberti, Yandong Yin, Julia K Pagan, Harrison Homer, Elizabeth Sassani, Andras Zeke, Luca Busino, Eli Rothenberg, Michele Pagano |
---|---|
Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2018-07-01
|
Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/38771 |
Similar Items
-
The Role of Tissue-Specific Ubiquitin Ligases, RNF183, RNF186, RNF182 and RNF152, in Disease and Biological Function
by: Takumi Okamoto, et al.
Published: (2020-05-01) -
The UAS thioredoxin-like domain of UBXN7 regulates E3 ubiquitin ligase activity of RNF111/Arkadia
by: Sadek Amhaz, et al.
Published: (2023-04-01) -
Put a RING on it: Regulation and inhibition of RNF8 and RNF168 RING finger E3 ligases at DNA damage sites.
by: Cristina eBartocci, et al.
Published: (2013-07-01) -
Regulation of p27 (Kip1) by Ubiquitin E3 Ligase RNF6
by: Dhanraj Deshmukh, et al.
Published: (2022-04-01) -
E3 ubiquitin ligase RNF180 prevents excessive PCDH10 methylation to suppress the proliferation and metastasis of gastric cancer cells by promoting ubiquitination of DNMT1
by: Nannan Zhang, et al.
Published: (2023-05-01)