IndraLab

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STAMBP deubiquitinates EGFR. 6 / 6
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"13 This implies that AMSH is able to completely deubiquitinate EGFR, since monoubiquitinated EGFR can still be targeted to lysosome."

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"STAMBP may deubiquitinate EGFR by localizing in early endosomes and increase EGFR membrane localization in LUAD cells."

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"AMSH can deubiquitinate EGFR and prompt recycling to the plasma membrane [XREF_BIBR], whilst USP8 is required for the degradation of EGFR in the lysosome [XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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"In support of this notion, we are able to show that EGFR, immunoprecipitated from EGF stimulated Her14 cells, can be deubiquitinated by AMSH in vitro."

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"AMSH was shown to deubiquitylate in vitro EGFR immunoprecipitated from EGF stimulated cells [XREF_BIBR], and siRNA knockdown of AMSH resulted in accelerated EGFR degradation in HeLa cells, which suggests that AMSH dependent deubiquitylation of EGFR counteracts Cbl dependent ubiquitylation of the receptor [XREF_BIBR]."

"AMSH (associated molecule with the SH3 domain of STAM) expression is elevated in many cancers and is capable of hydrolyzing K63-linked Ub chains from epidermal growth factor receptor (EGFR) recycling it to the plasma membrane"