scholarly journals FERONIA phosphorylates E3 ubiquitin ligase ATL6 to modulate the stability of 14-3-3 proteins in response to the carbon/nitrogen ratio

2019 ◽  
Vol 70 (21) ◽  
pp. 6375-6388 ◽  
Author(s):  
Guoyun Xu ◽  
Weijun Chen ◽  
Limei Song ◽  
Qiansi Chen ◽  
Hui Zhang ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Regulatory Mechanism ◽  
E3 Ubiquitin Ligase ◽  
Receptor Kinase ◽  
Carbon Nitrogen Ratio ◽  
Nitrogen Ratio ◽  
The Stability

This study reveals a novel regulatory mechanism that links the versatile receptor kinase FERONIA with plant C/N responses.

scholarly journals COP1 destabilizes DELLA proteins inArabidopsis

2020 ◽  
Vol 117 (24) ◽  
pp. 13792-13799 ◽  
Author(s):  
Noel Blanco-Touriñán ◽  
Martina Legris ◽  
Eugenio G. Minguet ◽  
Cecilia Costigliolo-Rojas ◽  
María A. Nohales ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Plant Cells ◽  
Transcriptional Regulators ◽  
Growth Responses ◽  
Warm Temperature ◽  
Della Proteins ◽  
The Stability ◽  
Dependent Pathway

DELLA transcriptional regulators are central components in the control of plant growth responses to the environment. This control is considered to be mediated by changes in the metabolism of the hormones gibberellins (GAs), which promote the degradation of DELLAs. However, here we show that warm temperature or shade reduced the stability of a GA-insensitive DELLA allele inArabidopsis thaliana. Furthermore, the degradation of DELLA induced by the warmth preceded changes in GA levels and depended on the E3 ubiquitin ligase CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1). COP1 enhanced the degradation of normal and GA-insensitive DELLA alleles when coexpressed inNicotiana benthamiana.DELLA proteins physically interacted with COP1 in yeast, mammalian, and plant cells. This interaction was enhanced by the COP1 complex partner SUPRESSOR OFphyA-1051 (SPA1). The level of ubiquitination of DELLA was enhanced by COP1 and COP1 ubiquitinated DELLA proteins in vitro. We propose that DELLAs are destabilized not only by the canonical GA-dependent pathway but also by COP1 and that this control is relevant for growth responses to shade and warm temperature.

Rlim, an E3 ubiquitin ligase, influences the stability of Stathmin protein in human osteosarcoma cells

2014 ◽  
Vol 26 (7) ◽  
pp. 1532-1538 ◽  
Author(s):  
Xi Chen ◽  
Jianjun Shen ◽  
Xingyu Li ◽  
Xi Wang ◽  
Min Long ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Osteosarcoma Cells ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cells ◽  
The Stability

scholarly journals The Hh pathway promotes cell apoptosis through Ci-Rdx-Diap1 axis

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Bin Liu ◽  
Yan Ding ◽  
Bing Sun ◽  
Qingxin Liu ◽  
Zizhang Zhou ◽  
...  
Keyword(s):  
Birth Defects ◽  
Ubiquitin Ligase ◽  
Cell Apoptosis ◽  
Target Gene ◽  
Regulatory Mechanism ◽  
E3 Ubiquitin Ligase ◽  
Human Diseases ◽  
Induced Apoptosis ◽  
Tumor Drugs ◽  
Transcriptional Target

AbstractApoptosis is a strictly coordinated process to eliminate superfluous or damaged cells, and its deregulation leads to birth defects and various human diseases. The regulatory mechanism underlying apoptosis still remains incompletely understood. To identify novel components in apoptosis, we carry out a modifier screen and find that the Hh pathway aggravates Hid-induced apoptosis. In addition, we reveal that the Hh pathway triggers apoptosis through its transcriptional target gene rdx, which encodes an E3 ubiquitin ligase. Rdx physically binds Diap1 to promote its K63-linked polyubiquitination, culminating in attenuating Diap1−Dronc interaction without affecting Diap1 stability. Taken together, our findings unexpectedly uncover the oncogenic Hh pathway is able to promote apoptosis through Ci-Rdx-Diap1 module, raising a concern to choose Hh pathway inhibitors as anti-tumor drugs.

scholarly journals The E3 ubiquitin ligase Pib1 regulates effective gluconeogenic shutdown in S. cerevisiae

2019 ◽  
Author(s):  
Vineeth Vengayil ◽  
Sunil Laxman
Keyword(s):  
Ubiquitin Ligase ◽  
Glucose Repression ◽  
E3 Ubiquitin Ligase ◽  
Proteasomal Degradation ◽  
Ubiquitin E3 Ligase ◽  
Nutrient Environment ◽  
The Stability ◽  
Glucose Availability

AbstractCells use multiple mechanisms to regulate their metabolic states depending on changes in their nutrient environment. A well-known example is the response of cells to glucose availability. In S. cerevisiae cells growing in glucose-limited medium, the re-availability of glucose leads to the downregulation of gluconeogenesis, the activation of glycolysis, and robust ‘glucose repression’. However, our knowledge of the initial mechanisms mediating this glucose-dependent downregulation of the gluconeogenic transcription factors is incomplete. We used the gluconeogenic transcription factor Rds2 as a candidate with which to discover regulators of early events leading to glucose repression. Here, we identify a novel role for the E3 ubiquitin ligase Pib1 in regulating the stability and degradation of Rds2. Glucose addition to glucose-limited cells results in rapid ubiquitination of Rds2, followed by its proteasomal degradation. Through in vivo and in vitro experiments, we establish Pib1 as a ubiquitin E3 ligase that regulates Rds2 ubiquitination and stability. Notably, this Pib1 mediated Rds2 ubiquitination, followed by proteasomal degradation, is specific to the presence of glucose. Pib1 is required for complete glucose repression, and enables cells to optimally grow in competitive environments when glucose becomes re-available. Our results reveal the existence of a Pib1 E3-ubiquitin ligase mediated regulatory program that mediates glucose-repression when glucose availability is restored.

scholarly journals Deubiquitinating enzymes Ubp2 and Ubp15 regulate endocytosis by limiting ubiquitination and degradation of ARTs

2017 ◽  
Vol 28 (9) ◽  
pp. 1271-1283 ◽  
Author(s):  
Hsuan-Chung Ho ◽  
Jason A. MacGurn ◽  
Scott D. Emr
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Protein Composition ◽  
Surface Proteins ◽  
Endocytic Pathway ◽  
Plasma Membrane Protein ◽  
Deubiquitinating Enzymes ◽  
Cell Surface Proteins ◽  
Cargo Proteins ◽  
The Stability

Endocytic down-regulation of cell-surface proteins is a fundamental cellular process for cell survival and adaptation to environmental stimuli. Ubiquitination of cargo proteins serves as the sorting signal for downstream trafficking and relies on the arrestin-related trafficking adaptor (ART)-Rsp5 ubiquitin ligase adaptor network in yeast. Hence proper regulation of the abundance and activity of these ligase–adaptor complexes is critical for main­tenance of optimal plasma membrane protein composition. Here we report that the stability of ARTs is regulated by the deubiquitinating enzymes (DUBs) Ubp2 and Ubp15. By counteracting the E3 ubiquitin ligase Rsp5, Ubp2 and Ubp15 prevent hyperubiquitination and proteasomal degradation of ARTs. Specifically, we show that loss of both Ubp2 and Ubp15 results in a defect in Hxt6 endocytosis associated with Art4 instability. Our results uncover a novel function for DUBs in the endocytic pathway by which Ubp2 and Ubp15 positively regulate the ART-Rsp5 network.

scholarly journals Stabilization of the E3 Ubiquitin Ligase Nrdp1 by the Deubiquitinating Enzyme USP8

2004 ◽  
Vol 24 (17) ◽  
pp. 7748-7757 ◽  
Author(s):  
Xiuli Wu ◽  
Lily Yen ◽  
Lisa Irwin ◽  
Colleen Sweeney ◽  
Kermit L. Carraway
Keyword(s):  
Ubiquitin Ligase ◽  
Tyrosine Kinases ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Growth Factor Receptor ◽  
Deubiquitinating Enzyme ◽  
Ubiquitin Ligase Activity ◽  
Apoptosis Protein ◽  
Epidermal Growth ◽  
The Stability

ABSTRACT Nrdp1 is a RING finger-containing E3 ubiquitin ligase that physically interacts with and regulates steady-state cellular levels of the ErbB3 and ErbB4 receptor tyrosine kinases and has been implicated in the degradation of the inhibitor-of-apoptosis protein BRUCE. Here we demonstrate that the Nrdp1 protein undergoes efficient proteasome-dependent degradation and that mutations in its RING finger domain that disrupt ubiquitin ligase activity enhance stability. These observations suggest that Nrdp1 self-ubiquitination and stability could play an important role in regulating the activity of this protein. Using affinity chromatography, we identified the deubiquitinating enzyme USP8 (also called Ubpy) as a protein that physically interacts with Nrdp1. Nrdp1 and USP8 could be coimmunoprecipitated, and in transfected cells USP8 specifically bound to Nrdp1 but not cbl, a RING finger E3 ligase involved in ligand-stimulated epidermal growth factor receptor down-regulation. The USP8 rhodanese and catalytic domains mediated Nrdp1 binding. USP8 markedly enhanced the stability of Nrdp1, and a point mutant that disrupts USP8 catalytic activity destabilized endogenous Nrdp1. Our results indicate that Nrdp1 is a specific target for the USP8 deubiquitinating enzyme and are consistent with a model where USP8 augments Nrdp1 activity by mediating its stabilization.

scholarly journals COP1 destabilizes DELLA proteins in Arabidopsis

2020 ◽  
Author(s):  
Noel Blanco-Touriñán ◽  
Martina Legris ◽  
Eugenio G. Minguet ◽  
Cecilia Costigliolo-Rojas ◽  
María A. Nohales ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Environmental Changes ◽  
Alternative Pathway ◽  
E3 Ubiquitin Ligase ◽  
Transcriptional Regulators ◽  
Transcriptional Networks ◽  
Growth Responses ◽  
Warm Temperature ◽  
Della Proteins ◽  
The Stability

AbstractDELLA transcriptional regulators are central components in the control of plant body form in response to the environment. This is considered to be mediated by changes in the metabolism of the hormones gibberellins (GAs), which promote the degradation of DELLAs. However, here we show that warm temperature or shade reduced the stability of a GA-insensitive DELLA allele in Arabidopsis. Furthermore, the degradation of DELLA induced by the warmth anticipated changes in GA levels and depended on the E3 ubiquitin ligase CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1). COP1 enhanced the degradation of normal and GA-insensitive DELLA alleles when co-expressed in N. benthamiana. DELLA proteins physically interacted with COP1 in yeast, mammalian and plant cells. This interaction was enhanced by the COP1 complex partner SUPRESSOR OF phyA-105 1 (SPA1). The level of ubiquitination of DELLA was enhanced by COP1 and COP1 ubiquitinated DELLA proteins in vitro. We propose that DELLAs are destabilized not only by the canonical GA-dependent pathway but also by COP1 and that this control is relevant for growth responses to shade and warm temperature.SignificanceDELLA proteins are plant-specific transcriptional regulators that act as signaling hubs at the interface between the environment and the transcriptional networks that control growth. DELLAs are destabilized by the growth-promoting hormone gibberellin, whose levels are very sensitive to environmental changes. Here we describe an alternative pathway to destabilize these proteins. We show that DELLAs are substrate of COP1, an E3 ubiquitin ligase that increases its nuclear activity to promote growth in response to shade or warmth. Our results also show that the destabilization of DELLAs by COP1 precedes the action of gibberellins, suggesting the existence of a sequential mechanism to control the stability of these proteins.

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