scholarly journals The E3 Ubiquitin Ligase SCFTIR1/AFB and Membrane Sterols Play Key Roles in Auxin Regulation of Endocytosis, Recycling, and Plasma Membrane Accumulation of the Auxin Efflux Transporter PIN2 in Arabidopsis thaliana

2009 ◽  
Vol 21 (2) ◽  
pp. 568-580 ◽  
Author(s):  
Jianwei Pan ◽  
Shozo Fujioka ◽  
Jianling Peng ◽  
Jianghua Chen ◽  
Guangming Li ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Plasma Membrane ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Efflux Transporter ◽  
Auxin Regulation

scholarly journals AtPUB19, a U-Box E3 Ubiquitin Ligase, Negatively Regulates Abscisic Acid and Drought Responses in Arabidopsis thaliana

2011 ◽  
Vol 4 (6) ◽  
pp. 938-946 ◽  
Author(s):  
Yong-Chang Liu ◽  
Yao-Rong Wu ◽  
Xia-He Huang ◽  
Jie Sun ◽  
Qi Xie
Keyword(s):  
Arabidopsis Thaliana ◽  
Abscisic Acid ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase

scholarly journals Regulation of Arabidopsis brassinosteroid receptor BRI1 endocytosis and degradation by plant U-box PUB12/PUB13-mediated ubiquitination

2018 ◽  
Vol 115 (8) ◽  
pp. E1906-E1915 ◽  
Author(s):  
Jinggeng Zhou ◽  
Derui Liu ◽  
Ping Wang ◽  
Xiyu Ma ◽  
Wenwei Lin ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Differentiation ◽  
Residence Time ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
E3 Ligase ◽  
Endocytic Pathway ◽  
Protein Abundance ◽  
Unique Mechanism

Plants largely rely on plasma membrane (PM)-resident receptor-like kinases (RLKs) to sense extracellular and intracellular stimuli and coordinate cell differentiation, growth, and immunity. Several RLKs have been shown to undergo internalization through the endocytic pathway with a poorly understood mechanism. Here, we show that endocytosis and protein abundance of the Arabidopsis brassinosteroid (BR) receptor, BR INSENSITIVE1 (BRI1), are regulated by plant U-box (PUB) E3 ubiquitin ligase PUB12- and PUB13-mediated ubiquitination. BR perception promotes BRI1 ubiquitination and association with PUB12 and PUB13 through phosphorylation at serine 344 residue. Loss of PUB12 and PUB13 results in reduced BRI1 ubiquitination and internalization accompanied with a prolonged BRI1 PM-residence time, indicating that ubiquitination of BRI1 by PUB12 and PUB13 is a key step in BRI1 endocytosis. Our studies provide a molecular link between BRI1 ubiquitination and internalization and reveal a unique mechanism of E3 ligase–substrate association regulated by phosphorylation.

scholarly journals Cul3-KLHL20 E3 ubiquitin ligase plays a key role in the arms race between HIV-1 and host restriction

2021 ◽  
Author(s):  
Rongrong Li ◽  
Iqbal Ahmad ◽  
Sunan Li ◽  
Silas Johnson ◽  
Liangliang Sun ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Productive Infection ◽  
Restriction Factors ◽  
Host Restriction ◽  
Host Restriction Factor ◽  
Cullin 3 ◽  
Golgi Network ◽  
Hiv 1

Abstract HIV-1 must counteract various host restriction factors to establish productive infection. SERINC5 is a critical host restriction factor that potently blocks HIV-1 entry from virions, but its activity is counteracted by Nef. The SERINC5 and Nef activities are both initiated from the plasma membrane, where SERINC5 is packaged into virions and downregulated by Nef via lysosomal degradation. However, it is still unclear how SERINC5 is localized to the plasma membrane and how its expression is regulated on the plasma membrane. We now report that Cullin 3-KLHL20, a trans-Golgi network (TGN)-localized E3 ubiquitin ligase, polyubiquitinates SERINC5 at lysine 130 via K33- and K48-linked ubiquitin chains. The K130 polyubiquitination is required not only for the SERINC5 expression on the plasma membrane, but also the SERINC5 anti-HIV-1 activity and the Nef counteractive activity. Our study reveals an important role of K33/K48-branched ubiquitin chains in HIV-1 infection by regulating protein post-Golgi trafficking and degradation.

scholarly journals The E3 Ubiquitin Ligase HOS1 Regulates Low Ambient Temperature-Responsive Flowering in Arabidopsis thaliana

2012 ◽  
Vol 53 (10) ◽  
pp. 1802-1814 ◽  
Author(s):  
Jeong Hwan Lee ◽  
Jae Joon Kim ◽  
Soo Hyun Kim ◽  
Hyun Jung Cho ◽  
Joonki Kim ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Ambient Temperature ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Temperature Responsive ◽  
Low Ambient Temperature

scholarly journals Endocytosis of the Aspartic Acid/Glutamic Acid Transporter Dip5 Is Triggered by Substrate-Dependent Recruitment of the Rsp5 Ubiquitin Ligase via the Arrestin-Like Protein Aly2

2010 ◽  
Vol 30 (24) ◽  
pp. 5598-5607 ◽  
Author(s):  
Riko Hatakeyama ◽  
Masao Kamiya ◽  
Terunao Takahara ◽  
Tatsuya Maeda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Acid Transporter ◽  
Py Motif ◽  
Related Proteins

ABSTRACT Endocytosis of nutrient transporters is stimulated under various conditions, such as elevated nutrient availability. In Saccharomyces cerevisiae, endocytosis is triggered by ubiquitination of transporters catalyzed by the E3 ubiquitin ligase Rsp5. However, how the ubiquitination is accelerated under certain conditions remains obscure. Here we demonstrate that closely related proteins Aly2/Art3 and Aly1/Art6, which are poorly characterized members of the arrestin-like protein family, mediate endocytosis of the aspartic acid/glutamic acid transporter Dip5. In aly2Δ cells, Dip5 is stabilized at the plasma membrane and is not endocytosed efficiently. Efficient ubiquitination of Dip5 is dependent on Aly2. aly1Δ cells also show deficiency in Dip5 endocytosis, although less remarkably than aly2Δ cells. Aly2 physically interacts in vivo with Rsp5 at its PY motif and also with Dip5, thus serving as an adaptor linking Rsp5 with Dip5 to achieve Dip5 ubiquitination. Importantly, the interaction between Aly2 and Dip5 is accelerated in response to elevated aspartic acid availability. This result indicates that the regulation of Dip5 endocytosis is accomplished by dynamic recruitment of Rsp5 via Aly2.

scholarly journals An IMiD-induced SALL4 degron system for selective degradation of target proteins

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Satoshi Yamanaka ◽  
Yuki Shoya ◽  
Saya Matsuoka ◽  
Hisayo Nishida-Fukuda ◽  
Norio Shibata ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Living Cells ◽  
Cellular Biology ◽  
Immunomodulatory Drugs ◽  
Unknown Mechanism ◽  
Selective Degradation ◽  
Ubiquitin Ligase Complex ◽  
Powerful Approach

AbstractRegulating the amount of proteins in living cells is a powerful approach for understanding the functions of the proteins. Immunomodulatory drugs (IMiDs) induce the degradation of neosubstrates by interacting with celebron (CRBN) in the cullin E3 ubiquitin ligase complex (CRL4CRBN). Here, we developed the IMiD-dependent Sal-like protein 4 (SALL4) degron (S4D) system for chemical protein knockdown. In transient assays, an N- or C-terminal S4D tag induced the degradation of proteins localized to various subcellular compartments, including the plasma membrane. The activity of luciferase-S4D was reduced by 90% within 3 h of IMiD treatment. IMiD treatment reduced the expression of endogenous S4D-fused RelA and IκBα in knock-in (KI) experiments. Interestingly, the IκBα knockdown suggested that there may be another, unknown mechanism for RelA translocation to the nucleus. Furthermore, 5-hydroxythalidomide as a thalidomide metabolite specifically degradated S4D-tagged protein. These results indicate that the S4D system is a useful tool for cellular biology.

scholarly journals C-terminal armadillo repeats are essential and sufficient for association of the plant U-box armadillo E3 ubiquitin ligase SAUL1 with the plasma membrane

2010 ◽  
Vol 62 (2) ◽  
pp. 775-785 ◽  
Author(s):  
Gabriele Drechsel ◽  
Johannes Bergler ◽  
Kathrin Wippel ◽  
Norbert Sauer ◽  
Katja Vogelmann ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Armadillo Repeats

AtARRE, an E3 ubiquitin ligase, negatively regulates ABA signaling in Arabidopsis thaliana

2018 ◽  
Vol 37 (9) ◽  
pp. 1269-1278 ◽  
Author(s):  
Boya Wang ◽  
Chuzhe Li ◽  
Xiangge Kong ◽  
Ying Li ◽  
Zhibin Liu ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Aba Signaling

scholarly journals Mindbomb 1, an E3 ubiquitin ligase, forms a complex with RYK to activate Wnt/β-catenin signaling

2011 ◽  
Vol 194 (5) ◽  
pp. 737-750 ◽  
Author(s):  
Jason D. Berndt ◽  
Atsushi Aoyagi ◽  
Peitzu Yang ◽  
Jamie N. Anastas ◽  
Lan Tang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Wnt Signaling ◽  
Ubiquitin Ligase ◽  
Genetic Interaction ◽  
E3 Ubiquitin Ligase ◽  
Secreted Protein ◽  
Loss Of Function ◽  
Protein Ligands ◽  
Steady State Levels ◽  
Novel Targets

Receptor-like tyrosine kinase (RYK) functions as a transmembrane receptor for the Wnt family of secreted protein ligands. Although RYK undergoes endocytosis in response to Wnt, the mechanisms that regulate its internalization and concomitant activation of Wnt signaling are unknown. We discovered that RYK both physically and functionally interacts with the E3 ubiquitin ligase Mindbomb 1 (MIB1). Overexpression of MIB1 promotes the ubiquitination of RYK and reduces its steady-state levels at the plasma membrane. Moreover, we show that MIB1 is sufficient to activate Wnt/β-catenin (CTNNB1) signaling and that this activity depends on endogenous RYK. Conversely, in loss-of-function studies, both RYK and MIB1 are required for Wnt-3A–mediated activation of CTNNB1. Finally, we identify the Caenorhabditis elegans orthologue of MIB1 and demonstrate a genetic interaction between ceMIB and lin-18/RYK in vulva development. These findings provide insights into the mechanisms of Wnt/RYK signaling and point to novel targets for the modulation of Wnt signaling.

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