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USP8 deubiquitinates EGFR. 16 / 16
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"USP8 (also known as UBPY) deubiquitylates EGFR on early endosomes, rescuing EGFR from degradation 107, 108 ."

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"Before incorporation into MVBs, the EGFR is deubiquitinated by Usp8."

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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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"Based on these studies, we propose a model whereby the concerted recruitment of CHMP4B and UBPY to HD-PTP and the engagement of UBPY by STAM2 displaces ESCRT-0 from HD-PTP, deubiquitinates EGFR, and releases ESCRT-0 from cargo in favor of ESCRT-III."

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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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"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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"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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"Immunopurified UBPY deubiquitinated EGFR in vitro."

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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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"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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"USP8 (also known as UBPY) deubiquitylates EGFR on early endosomes, rescuing EGFR from degradation ."

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"Although still a matter of debate, EGFR deubiquitination by the ESCRTassociated deubiquitinating (DUB) enzyme UBPY (ubiquitinspecific protease 8) appears to facilitate the transfer of activated EGFRs from early ubiquitin-binding ESCRT complexes (ESCRT-0, -I, -II) to ESCRT-III (Mizuno et al., 2005; Row et al., 2006; Alwan and van Leeuwen, 2007) ."

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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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"Although USP8 promotes epidermal growth factor receptor (EGFR) deubiquitination, its role in ESCRT-mediated endosomal sorting of RTKs remains controversial."

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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]."