scholarly journals The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor

2013 ◽  
Vol 126 (6) ◽  
pp. 1366-1380 ◽  
Author(s):  
C. J. Smith ◽  
D. M. Berry ◽  
C. J. McGlade
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Endosomal Sorting ◽  
Epidermal Growth

scholarly journals SCAMP3 Negatively Regulates Epidermal Growth Factor Receptor Degradation and Promotes Receptor Recycling

2009 ◽  
Vol 20 (6) ◽  
pp. 1816-1832 ◽  
Author(s):  
Quyen L. Aoh ◽  
Anna M. Castle ◽  
Charles H. Hubbard ◽  
Osamu Katsumata ◽  
J. David Castle
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Multivesicular Bodies ◽  
Receptor Recycling ◽  
Endosomal Sorting ◽  
Accelerated Degradation ◽  
Early Endosomes ◽  
Epidermal Growth

The epidermal growth factor receptor (EGFR) is targeted for lysosomal degradation by ubiquitin-mediated interactions with the ESCRTs (endosomal-sorting complexes required for transport) in multivesicular bodies (MVBs). We show that secretory carrier membrane protein, SCAMP3, localizes in part to early endosomes and negatively regulates EGFR degradation through processes that involve its ubiquitylation and interactions with ESCRTs. SCAMP3 is multimonoubiquitylated and is able to associate with Nedd4 HECT ubiquitin ligases and the ESCRT-I subunit Tsg101 via its PY and PSAP motifs, respectively. SCAMP3 also associates with the ESCRT-0 subunit Hrs. Depletion of SCAMP3 in HeLa cells by inhibitory RNA accelerated degradation of EGFR and EGF while inhibiting recycling. Conversely, overexpression enhanced EGFR recycling unless ubiquitylatable lysines, PY or PSAP motifs in SCAMP3 were mutated. Notably, dual depletions of SCAMP3 and ESCRT subunits suggest that SCAMP3 has a distinct function in parallel with the ESCRTs that regulates receptor degradation. This function may affect trafficking of receptors from prelysosomal compartments as SCAMP3 depletion appeared to sustain the incidence of EGFR-containing MVBs detected by immunoelectron microscopy. Together, our results suggest that SCAMP3, its modification with ubiquitin, and its interactions with ESCRTs coordinately regulate endosomal pathways and affect the efficiency of receptor down-regulation.

scholarly journals Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway

FEBS Journal ◽  
2014 ◽  
Vol 281 (16) ◽  
pp. 3642-3655 ◽  
Author(s):  
Yuki Maemoto ◽  
Yasuko Ono ◽  
Satomi Kiso ◽  
Hideki Shibata ◽  
Terunao Takahara ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Endosomal Sorting ◽  
Epidermal Growth

scholarly journals Gαs protein binds ubiquitin to regulate epidermal growth factor receptor endosomal sorting

2017 ◽  
Vol 114 (51) ◽  
pp. 13477-13482 ◽  
Author(s):  
Xuezhi Li ◽  
Danny Létourneau ◽  
Brian Holleran ◽  
Richard Leduc ◽  
Pierre Lavigne ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cellular Response ◽  
Growth Factor Receptor ◽  
Fine Tuning ◽  
Lysosomal Degradation ◽  
Endosomal Sorting ◽  
Epidermal Growth ◽  
G Protein Coupled

The Gαs subunit is classically involved in the signal transduction of G protein-coupled receptors (GPCRs) at the plasma membrane. Recent evidence has revealed noncanonical roles for Gαs in endosomal sorting of receptors to lysosomes. However, the mechanism of action of Gαs in this sorting step is still poorly characterized. Here, we report that Gαs interacts with ubiquitin to regulate the endosomal sorting of receptors for lysosomal degradation. We reveal that the N-terminal extremity of Gαs contains a ubiquitin-interacting motif (UIM), a sorting element usually found in the endosomal sorting complex required for transport (ESCRT) machinery responsible for sorting ubiquitinated receptors into intraluminal vesicles (ILVs) of multivesicular bodies (MVBs). Mutation of the UIM in Gαs confirmed the importance of ubiquitin interaction for the sorting of epidermal growth factor receptor (EGFR) into ILVs for lysosomal degradation. These findings demonstrate a role for Gαs as an integral component of the ubiquitin-dependent endosomal sorting machinery and highlight the dual role of Gαs in receptor trafficking and signaling for the fine-tuning of the cellular response.

A role for Hrs in endosomal sorting of ligand-stimulated and unstimulated epidermal growth factor receptor

2004 ◽  
Vol 297 (2) ◽  
pp. 380-391 ◽  
Author(s):  
Chitose Morino ◽  
Masaki Kato ◽  
Akitsugu Yamamoto ◽  
Emi Mizuno ◽  
Akira Hayakawa ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Endosomal Sorting ◽  
Epidermal Growth

scholarly journals Bcr Interacts with Components of the Endosomal Sorting Complex Required for Transport-I and Is Required for Epidermal Growth Factor Receptor Turnover

2006 ◽  
Vol 66 (12) ◽  
pp. 6250-6257 ◽  
Author(s):  
Oyenike O. Olabisi ◽  
Gwendolyn M. Mahon ◽  
Elena V. Kostenko ◽  
Zhuoming Liu ◽  
Harvey L. Ozer ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Endosomal Sorting ◽  
Epidermal Growth ◽  
Receptor Turnover
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