Results 31 to 40 of about 211,577 (291)

Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation

Nature Communications, 2022
The GID E3 ligase regulates glucose-induced degradation in yeast, and key physiology. This study unveils E3 ligase regulation by reshaping the substrate binding site, blocking substrate access to ubiquitination active sites, and a Cage-like assembly.
Shuai Qiao, Chia-Wei Lee, Dawafuti Sherpa, Jakub Chrustowicz, Jingdong Cheng, Maximilian Duennebacke, Barbara Steigenberger, Ozge Karayel, Duc Tung Vu, Susanne von Gronau, Matthias Mann, Florian Wilfling, Brenda A. Schulman   +12 more
doaj   +1 more source

Genome-Wide Identification of the U-Box E3 Ubiquitin Ligase Gene Family in Cabbage (Brassica oleracea var. capitata) and Its Expression Analysis in Response to Cold Stress and Pathogen Infection

Plants, 2023
Plant U-box E3 ubiquitin ligases (PUBs) play an important role in growth, development, and stress responses in many species. However, the characteristics of U-box E3 ubiquitin ligase genes in cabbage (Brassica oleracea var.
Peiwen Wang, Lin Zhu, Ziheng Li, Mozhen Cheng, Xiuling Chen, Aoxue Wang, Chao Wang, Xiaoxuan Zhang   +7 more
doaj   +1 more source

Ubiquitin E3 ligase activity of Ralstonia solanacearum effector RipAW is not essential for induction of plant defense in Nicotiana benthamiana

Frontiers in Microbiology, 2023
As one of the most destructive bacterial phytopathogens, Ralstonia solanacearum causes substantial annual yield losses of many important crops. Deciphering the functional mechanisms of type III effectors, the crucial factors mediating R.
Xue Ouyang, Jialan Chen, Zhimao Sun, Rongbo Wang, Xuan Wu, Benjin Li, Congfeng Song, Peiqing Liu, Meixiang Zhang   +8 more
doaj   +1 more source

A pathogen type III effector with a novel E3 ubiquitin ligase architecture.

PLoS Pathogens, 2013
Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression.
Alexander U Singer, Sebastian Schulze, Tatiana Skarina, Xiaohui Xu, Hong Cui, Lennart Eschen-Lippold, Monique Egler, Tharan Srikumar, Brian Raught, Justin Lee, Dierk Scheel, Alexei Savchenko, Ulla Bonas   +12 more
doaj   +1 more source

RING Domain E3 Ubiquitin Ligases

Annual Review of Biochemistry, 2009
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2∼ubiquitin thioester and activates discharge of its ubiquitin cargo.
Deshaies, Raymond J., Joazeiro, Claudio A. P.   +1 more
openaire   +3 more sources

Genome-wide identification and transcriptome profiling reveal that E3 ubiquitin ligase genes relevant to ethylene, auxin and abscisic acid are differentially expressed in the fruits of melting flesh and stony hard peach varieties

BMC Genomics, 2019
Background Ubiquitin ligases (E3) are the enzymes in the ubiquitin/26S proteasome pathway responsible for targeting proteins to the degradation pathway and play major roles in multiple biological activities. However, the E3 family and their functions are
Bin Tan, Xiaodong Lian, Jun Cheng, Wenfang Zeng, Xianbo Zheng, Wei Wang, Xia Ye, Jidong Li, Zhiqian Li, Langlang Zhang, Jiancan Feng   +10 more
doaj   +1 more source

Regulating the human HECT E3 ligases [PDF]

Cellular and Molecular Life Sciences, 2018
Ubiquitination, the covalent attachment of ubiquitin to proteins, by E3 ligases of the HECT (homologous to E6AP C terminus) family is critical in controlling diverse physiological pathways. Stringent control of HECT E3 ligase activity and substrate specificity is essential for cellular health, whereas deregulation of HECT E3s plays a prominent role in ...
Sluimer, Jasper, Distel, Ben
openaire   +4 more sources

Trim25 restricts rabies virus replication by destabilizing phosphoprotein

Cell Insight, 2022
Tripartite motif-containing protein 25 (Trim25) is an E3 ubiquitin ligase that activates retinoid acid-inducible gene I (RIG-I) and promotes the antiviral interferon response.
Yueming Yuan, An Fang, Zongmei Wang, Bin Tian, Yuan Zhang, Baokun Sui, Zhaochen Luo, Yingying Li, Ming Zhou, Huanchun Chen, Zhen F. Fu, Ling Zhao   +11 more
doaj   +1 more source

Stress response silencing by an E3 ligase mutated in neurodegeneration

Nature
Stress response pathways detect and alleviate adverse conditions to safeguard cell and tissue homeostasis, yet their prolonged activation induces apoptosis and disrupts organismal health1–3. How stress responses are turned off at the right time and place
Diane L. Haakonsen, Michael Heider, Andrew J Ingersoll, Kayla Vodehnal, Samuel R Witus, Takeshi Uenaka, Marius Wernig, Michael Rapé   +7 more
semanticscholar   +1 more source

A caged E3 ligase ligand for PROTAC-mediated protein degradation with light.

Chemical Communications, 2020
With the intent of achieving greater spatiotemporal control of PROTAC-induced protein degradation, a light-activated degrader was designed by photocaging an essential E3 ligase binding motif in a BRD4 targeting PROTAC.
C. Kounde, Maria M. Shchepinova, Charlie N. Saunders, M. Muelbaier, M. Rackham, J. Harling, Edward W. Tate   +6 more
semanticscholar   +1 more source