Faculty Opinions recommendation of Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCF-Cdc34.

2006 ◽  
Author(s):  
Jane Endicott
Keyword(s):  
Ubiquitin Ligase ◽  
Ubiquitin Chain ◽  
Ubiquitin Ligase Complex ◽  
Chain Synthesis

scholarly journals SCFFbl12Increases p21Waf1/Cip1Expression Level through Atypical Ubiquitin Chain Synthesis

2016 ◽  
Vol 36 (16) ◽  
pp. 2182-2194 ◽  
Author(s):  
Fuminori Tsuruta ◽  
Ai Takebe ◽  
Kousuke Haratake ◽  
Yoshinori Kanemori ◽  
Jaehyun Kim ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Tumor Development ◽  
Cdk Inhibitor ◽  
Cyclin Dependent Kinase ◽  
Ubiquitin Chain ◽  
Proteasome Activator ◽  
Key Factor ◽  
Scf Ubiquitin Ligase ◽  
Chain Synthesis ◽  
Unstructured Protein

The cyclin-dependent kinase (CDK) inhibitor p21 is an unstructured protein regulated by multiple turnover pathways. p21 abundance is tightly regulated, and its defect causes tumor development. However, the mechanisms that underlie the control of p21 level are not fully understood. Here, we report a novel mechanism by which a component of the SCF ubiquitin ligase, Fbl12, augments p21 via the formation of atypical ubiquitin chains. We found that Fbl12 binds and ubiquitinates p21. Unexpectedly, Fbl12 increases the expression level of p21 by enhancing the mixed-type ubiquitination, including not only K48- but also K63-linked ubiquitin chains, followed by promotion of binding between p21 and CDK2. We also found that proteasome activator PA28γ attenuates p21 ubiquitination by interacting with Fbl12. In addition, UV irradiation induces a dissociation of p21 from Fbl12 and decreases K63-linked ubiquitination, leading to p21 degradation. These data suggest that Fbl12 is a key factor that maintains adequate intracellular concentration of p21 under normal conditions. Our finding may provide a novel possibility that p21's fate is governed by diverse ubiquitin chains.

scholarly journals Ubiquitin-dependent regulation of immune and inflammatory signaling pathways

2014 ◽  
Vol 70 (a1) ◽  
pp. C241-C241
Author(s):  
Katrin Rittinger
Keyword(s):  
Signaling Pathways ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
High Specificity ◽  
Cellular Functions ◽  
Inflammatory Signaling ◽  
Ubiquitin Chain ◽  
E3 Ligases ◽  
Wide Range ◽  
Chain Synthesis

Modification of proteins with ubiquitin is a key mechanism for the regulation of a wide range of cellular functions. The outcome of the modification is determined by the way ubiquitin molecules are linked to each other. Linear (M1-linked) ubiquitin chains play an important role in the regulation of immune and inflammatory signaling pathways and contribute to the activation of NF-κB. They are synthesized by the E3 ubiquitin ligase LUBAC (linear ubiquitin chain assembly complex) that is composed of at least three subunits named HOIL-1L, HOIP and SHARPIN. LUBAC belongs to the RBR (RING-inbetween-RING) family of E3 ligases that combine the properties of RING and HECT ligases and act as RING/HECT hybrids. Indeed, we have recently shown that linear ubiquitin chain synthesis proceeds via ubiquitin thioester intermediate formed by the HOIP subunit before subsequent transfer onto the target. I will present a combination of structural and biochemical data that provide a molecular explanation how this unusual E3 ligase complex promotes the synthesis of linear ubiquitin chains with high specificity, regardless of the E2 conjugating enzyme it works with.

scholarly journals Mechanism of ubiquitin chain synthesis employed by a HECT domain ubiquitin ligase

2017 ◽  
Vol 292 (25) ◽  
pp. 10398-10413 ◽  
Author(s):  
Michael E. French ◽  
Julian L. Klosowiak ◽  
Aaron Aslanian ◽  
Steven I. Reed ◽  
John R. Yates ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Ubiquitin Chain ◽  
Hect Domain ◽  
Chain Synthesis

COI1 links jasmonate signalling and fertility to the SCF ubiquitin-ligase complex inArabidopsis

2002 ◽  
Vol 32 (4) ◽  
pp. 457-466 ◽  
Author(s):  
Alessandra Devoto ◽  
Manuela Nieto-Rostro ◽  
Daoxin Xie ◽  
Christine Ellis ◽  
Rebecca Harmston ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Ubiquitin Ligase Complex ◽  
Scf Ubiquitin Ligase ◽  
Jasmonate Signalling

scholarly journals Correction: A Ubiquitin Ligase Complex Regulates Caspase Activation During Sperm Differentiation in Drosophila

PLoS Biology ◽  
2007 ◽  
Vol 5 (11) ◽  
pp. e291
Author(s):  
Eli Arama ◽  
Maya Bader ◽  
Gabrielle E Rieckhof ◽  
Hermann Stellar
Keyword(s):  
Ubiquitin Ligase ◽  
Caspase Activation ◽  
Ubiquitin Ligase Complex
Sign in / Sign up

Export Citation Format

Share Document