IndraLab

Statements

USP8 deubiquitinates EGFR. 24 / 24
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"Some studies showed that AMSH [31] and UBPY [32, 33] prevent EGFR down-regulation by deubiquitinating EGFR."
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"USP8 (also known as UBPY) deubiquitylates EGFR on early endosomes, rescuing EGFR from degradation ."
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"In a subset of Cushing tumors, a mutant ubiquitin-specific protease 8 (USP8) leads to attenuated EGFR ubiquitination and degradation (9, 10)."
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"Previous studies have shown that the recruitment of USP8/UBPY to the ESCRT-III complex deubiquitinates EGFR and thereby drives EGFR into ILVs, which fuse with lysosomes for further degradation ."
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"By deubiquitinating EGFR on endosomes, USP8 prevents EGFR from degrading in lysosomes and reduces the rate of EGFR down-regulation after being stimulated with EGF [26,27] ."
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"Loss of UBPY function enhances EGFR ubiquitination, but studies differ in their conclusions about how this affects EGFR trafficking [19, 23-29]."
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"Gain-of-function mutations in USP8 increase the deubiquitination of EGFR, which inhibits its degradation, leading to the activation of EGFR signaling."
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"Furthermore we demonstrated that both EGFR and EGFR-ErbB2 TM are deubiquitinated by the deubiquitination enzyme Usp8, although deubiquitination of ErbB2 was less efficient than that of EGFR [10]."
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"Here, we describe the role of a deubiquitinating enzyme UBPY/USP8 in the down-regulation of epidermal growth factor (EGF) receptor (EGFR). Overexpression of UBPY reduced the ubiquitination level of EGFR and delayed its degradation in EGF-stimulated cells."
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"If USP8 deubiquitylates EGFR at the MVB, this facilitates EGFR 's progression toward degradation in the lysosome and, thus, aids receptor down-regulation."
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"Although USP8 promotes epidermal growth factor receptor (EGFR) deubiquitination, its role in ESCRT-mediated endosomal sorting of RTKs remains controversial."
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"They are located at the 14-3-3 binding motif, and the mutations disrupt the binding between USP8 and 14-3-3 protein, which leads to increased deubiquitination and EGFR signaling."
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"All these findings are in favor of a model whereby USP8 promotes EGFR de-ubiquitination and degradation and is required for lysosomal sorting (see [57] for a review)."
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"Immunopurified UBPY deubiquitinated EGFR in vitro."
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"27775833"
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"In normal conditions, USP8 deubiquitinates various proteins, including EGFR, and prevents their lysosomal degradation [47,48]."
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"However, we can not fully exclude the other possibility that the UBPY S680A expression resulted in a reduction in the cellular Ub conjugating activity toward activated EGFR in some way.The fact that U[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In an elegant and comprehensive analysis of corticotroph adenoma, Reincke et al demonstrated that heterozygous somatic USP8 single nucleotide mutation or deletions at or adjacent to the 14-3-3 protein binding domain make USP8 resistant to 14-3-3 protein binding and more prone to proteolytic cleavage, which, in turn, leads to higher rate of USP8 induced EGFR deubiquitination activity upon binding of EGF to its receptor."
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"USP8 is known to deubiquitinate EGFR in response to ligand stimulation. USP8 depletion accelerates receptor turnover, whereas loss of hepatocyte growth factor-regulated substrate (Hrs) rescues this phenotype, indicating that USP8 protects EGFR from degradation via an Hrs-dependent pathway. [..]As EGFR stabilization against lysosomal turnover requires deubiquitination by USP8."
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"Besides it is also important to mention that USP8 inhibits EGFR ubiquitination and thus inhibits proteasome-mediated EGFR degradation [ 40 , 41 ]."
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"While AMSH is required for sorting of EGFR into MVEs and degradation in lysosomes XREF_BIBR, deubiquitination of EGFR by USP8 protects it from lysosomal degradation XREF_BIBR."
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"It is already known that the EGFR is deubiquitinated and stabilized by cleaved USP8 (activated form) leading to increase EGF mediated downstream signaling [ 7 , 10 ]."
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"USP8 mediates the deubiquitination of EGFR by inhibiting its interaction with protein 14-3-3, which in turn prevents its proteosomal degradation."
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"Some siRNA studies suggest that Usp8/UbpY-dependent deubiquitination of EGFR promotes further trafficking to the lysosome and EGFR degradation [ 66,67 ]."
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