scholarly journals The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCFSkp2

2002 ◽  
Vol 16 (22) ◽  
pp. 2946-2957 ◽  
Author(s):  
D. Tedesco
Keyword(s):  
Ubiquitin Ligase ◽  
Related Protein

scholarly journals The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis

2018 ◽  
Vol 29 (9) ◽  
pp. 1012-1020 ◽  
Author(s):  
Junie Hovsepian ◽  
Véronique Albanèse ◽  
Michel Becuwe ◽  
Vasyl Ivashov ◽  
David Teis ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Endocytic Pathway ◽  
Yeast Cells ◽  
Monocarboxylate Transporter ◽  
Related Protein ◽  
Related Family ◽  
Nutrient Signaling ◽  
Mechanistic Basis ◽  
A Current ◽  
Glucose Availability

Yeast cells have a remarkable ability to adapt to nutritional changes in their environment. During adaptation, nutrient-signaling pathways drive the selective endocytosis of nutrient transporters present at the cell surface. A current challenge is to understand the mechanistic basis of this regulation. Transporter endocytosis is triggered by their ubiquitylation, which involves the ubiquitin ligase Rsp5 and its adaptors of the arrestin-related family (ART). This step is highly regulated by nutrient availability. For instance, the monocarboxylate transporter Jen1 is ubiquitylated, endocytosed, and degraded upon exposure to glucose. The ART protein Rod1 is required for this overall process; yet Rod1 rather controls Jen1 trafficking later in the endocytic pathway and is almost dispensable for Jen1 internalization. Thus, how glucose triggers Jen1 internalization remains unclear. We report that another ART named Bul1, but not its paralogue Bul2, contributes to Jen1 internalization. Bul1 responds to glucose availability, and preferentially acts at the plasma membrane for Jen1 internalization. Thus, multiple ARTs can act sequentially along the endocytic pathway to control transporter homeostasis. Moreover, Bul1 is in charge of Jen1 endocytosis after cycloheximide treatment, suggesting that the functional redundancy of ARTs may be explained by their ability to interact with multiple cargoes in various conditions.

scholarly journals SIP/CacyBP promotes autophagy by regulating levels of BRUCE/Apollon, which stimulates LC3-I degradation

2019 ◽  
Vol 116 (27) ◽  
pp. 13404-13413 ◽  
Author(s):  
Tian-Xia Jiang ◽  
Jiang-Bo Zou ◽  
Qian-Qian Zhu ◽  
Cui Hua Liu ◽  
Guang-Fei Wang ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Cultured Cells ◽  
Proteasomal Degradation ◽  
Related Protein ◽  
Topoisomerase Inhibitors ◽  
Autophagosome Formation ◽  
Recycling Endosome ◽  
Proteasome Activator ◽  
Apoptosis Protein ◽  
Autophagic Degradation

BRUCE/Apollon is a membrane-associated inhibitor of apoptosis protein that is essential for viability and has ubiquitin-conjugating activity. On initiation of apoptosis, the ubiquitin ligase Nrdp1/RNF41 promotes proteasomal degradation of BRUCE. Here we demonstrate that BRUCE together with the proteasome activator PA28γ causes proteasomal degradation of LC3-I and thus inhibits autophagy. LC3-I on the phagophore membrane is conjugated to phosphatidylethanolamine to form LC3-II, which is required for the formation of autophagosomes and selective recruitment of substrates. SIP/CacyBP is a ubiquitination-related protein that is highly expressed in neurons and various tumors. Under normal conditions, SIP inhibits the ubiquitination and degradation of BRUCE, probably by blocking the binding of Nrdp1 to BRUCE. On DNA damage by topoisomerase inhibitors, Nrdp1 causes monoubiquitination of SIP and thus promotes apoptosis. However, on starvation, SIP together with Rab8 enhances the translocation of BRUCE into the recycling endosome, formation of autophagosomes, and degradation of BRUCE by optineurin-mediated autophagy. Accordingly, deletion of SIP in cultured cells reduces the autophagic degradation of damaged mitochondria and cytosolic protein aggregates. Thus, by stimulating proteasomal degradation of LC3-I, BRUCE also inhibits autophagy. Conversely, SIP promotes autophagy by blocking BRUCE-dependent degradation of LC3-I and by enhancing autophagosome formation and autophagic destruction of BRUCE. These actions of BRUCE and SIP represent mechanisms that link the regulation of autophagy and apoptosis under different conditions.

scholarly journals A Mechanism for Protein Monoubiquitination Dependent on a trans-Acting Ubiquitin-binding Domain

2013 ◽  
Vol 288 (23) ◽  
pp. 16206-16211 ◽  
Author(s):  
Antonio Herrador ◽  
Sébastien Léon ◽  
Rosine Haguenauer-Tsapis ◽  
Olivier Vincent
Keyword(s):  
Chain Length ◽  
Ubiquitin Ligase ◽  
Functional Outcomes ◽  
Binding Domain ◽  
Chain Elongation ◽  
Related Protein ◽  
Ubiquitin Chain ◽  
Ubiquitin Binding ◽  
Ubiquitin Binding Domain

The length of the ubiquitin chain on a substrate dictates various functional outcomes, yet little is known about its regulation in vivo. The yeast arrestin-related protein Rim8/Art9 is monoubiquitinated in vivo by the Rsp5 ubiquitin ligase. This also requires Vps23, a protein that displays an ubiquitin-E2 variant (UEV) domain. Here, we report that binding of the UEV domain to Rim8 interferes with ubiquitin chain elongation and directs Rim8 monoubiquitination. We propose that Vps23 UEV competes with Rsp5 HECT N-lobe for binding to the first conjugated ubiquitin, thereby preventing polyubiquitination. These findings reveal a novel mechanism to control ubiquitin chain length on substrates in vivo.

scholarly journals Integrated control of transporter endocytosis and recycling by the arrestin-related protein Rod1 and the ubiquitin ligase Rsp5

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Michel Becuwe ◽  
Sébastien Léon
Keyword(s):  
Ubiquitin Ligase ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Integrated Control ◽  
Monocarboxylate Transporter ◽  
Related Protein ◽  
Endocytic Sorting ◽  
Lysosomal Targeting ◽  
Golgi Network ◽  
External Signals

After endocytosis, membrane proteins can recycle to the cell membrane or be degraded in lysosomes. Cargo ubiquitylation favors their lysosomal targeting and can be regulated by external signals, but the mechanism is ill-defined. Here, we studied the post-endocytic trafficking of Jen1, a yeast monocarboxylate transporter, using microfluidics-assisted live-cell imaging. We show that the ubiquitin ligase Rsp5 and the glucose-regulated arrestin-related trafficking adaptors (ART) protein Rod1, involved in the glucose-induced internalization of Jen1, are also required for the post-endocytic sorting of Jen1 to the yeast lysosome. This new step takes place at the trans-Golgi network (TGN), where Rod1 localizes dynamically upon triggering endocytosis. Indeed, transporter trafficking to the TGN after internalization is required for their degradation. Glucose removal promotes Rod1 relocalization to the cytosol and Jen1 deubiquitylation, allowing transporter recycling when the signal is only transient. Therefore, nutrient availability regulates transporter fate through the localization of the ART/Rsp5 ubiquitylation complex at the TGN.

scholarly journals Recruitment of the ESCRT Machinery to a Putative Seven-Transmembrane-Domain Receptor Is Mediated by an Arrestin-Related Protein

2009 ◽  
Vol 30 (4) ◽  
pp. 897-907 ◽  
Author(s):  
Antonio Herrador ◽  
Silvia Herranz ◽  
David Lara ◽  
Olivier Vincent
Keyword(s):  
Ubiquitin Ligase ◽  
Transmembrane Domain ◽  
Ph Sensor ◽  
E3 Ubiquitin Ligase ◽  
Related Protein ◽  
Animal Cells ◽  
Gag Proteins ◽  
Endosomal Sorting ◽  
Escrt Machinery ◽  
7Tm Receptors

ABSTRACT Mammalian arrestins have a major role in the intracellular trafficking of seven-transmembrane (7TM) receptors. The fungal ambient pH signaling pathway involves an arrestin-related protein, PalF/Rim8, and the ESCRT (endosomal sorting complex required for transport) machinery. We found that in Saccharomyces cerevisiae, Rim8 binds to both the putative 7TM pH sensor Rim21 and the ESCRT-I subunit Vps23. We show that an SXP motif in Rim8 mediates binding to the Vps23 ubiquitin E2 variant (UEV) domain and that a monoubiquitinated residue near the SXP motif contributes to this interaction. We present evidence that Rim8 ubiquitination is dependent on the Rsp5 E3 ubiquitin ligase and triggered upon binding of Vps23 UEV to both the SXP motif and ubiquitin, thus suggesting a two-step binding mechanism. We further show that Rim8 coimmunoprecipitates with ESCRT-I subunits Vps23 and Vps28, supporting the idea that binding of Rim8 to Vps23 mediates the association of Rim8 with the ESCRT-I complex. Fluorescence microscopic analyses indicate that overexpressed Rim8 and Vps23 colocalize at cortical punctate structures, providing additional evidence of the interaction between these two proteins. Strikingly, our findings indicate that evolutionary conserved mechanisms control the recruitment of the ESCRT machinery to Pal/Rim proteins in fungi and retroviral Gag proteins in animal cells.

scholarly journals Cancer stem-like cell related protein CD166 degrades through E3 ubiquitin ligase CHIP in head and neck cancer

2017 ◽  
Vol 353 (1) ◽  
pp. 46-53 ◽  
Author(s):  
Meng Xiao ◽  
Ming Yan ◽  
Jianjun Zhang ◽  
Qin Xu ◽  
Shengcai Qi ◽  
...  
Keyword(s):  
Head And Neck Cancer ◽  
Head And Neck ◽  
Neck Cancer ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Related Protein

scholarly journals The inositol phosphatase MTMR4 is a novel target of the ubiquitin ligase Nedd4

2009 ◽  
Vol 419 (1) ◽  
pp. 57-63 ◽  
Author(s):  
Pamela J. Plant ◽  
Judy Correa ◽  
Neil Goldenberg ◽  
James Bain ◽  
Jane Batt
Keyword(s):  
Ubiquitin Ligase ◽  
Biological Process ◽  
Precursor Cell ◽  
Neural Precursor ◽  
Neural Precursor Cell ◽  
Related Protein ◽  
Inositol Phosphatase ◽  
Late Endosomes ◽  
Muscle Breakdown ◽  
Novel Target

The inositol phosphatase, MTMR4 (myotubularin-related protein 4), was identified as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4). hMTMR4 (human MTMR4) and Nedd4 co-immunoprecipitated and co-localized to late endosomes. The PY (Pro-Tyr) motif of hMTMR4 binds to WW (Trp-Trp) domains of hNedd4. MTMR4 expression was decreased in atrophying muscle, whereas Nedd4 expression was increased and hMTMR4 was ubiquitinated by hNedd4, suggesting that this novel interaction may underlie the biological process of muscle breakdown.

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