IndraLab

Statements

USP8 binds ERBB2. 11 / 13
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"Our current findings further demonstrate that Usp8 binds to ErbB2 and that Usp8 tyrosine phosphorylation is dependent on ErbB2- ( Fig. 4 ) and Src- kinase ( Fig. 5 ) activities, thereby extending our [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Further data confirmed that PAK5 enhanced the interaction between HER2 and USP8 via MALAT1 (Fig. 3H)."
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"The stabilized MALAT1 inhibits ubiquitin-proteasomal degradation of the N-HER2 by affecting the interaction of deubiquitinase USP8 and N-HER2, thereby promoting N-HER2 accumulation."
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"We also found that PAK5 WT but not PAK5 KM enhanced the interaction between deubiquitinase USP8 and N-HER2 (Fig. xref )."
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"Given the impaired downregulation of ErbB2, we have investigated in the present study whether ErbB2 and Usp8 functionally interact."
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"The increased expression of MALAT1 enhances the binding of deubiquitinase USP8 to N-HER2, which inhibits the N-HER2 ubiquitin proteasomal degradation, leading to the N-HER2 accumulation."
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"Moreover, MALAT1 inhibits ubiquitin-proteasomal degradation of the N-HER2 by affecting the binding of deubiquitinase USP8 and N-HER2, thereby promoting N-HER2 accumulation and trastuzumab resistance in HER2-positive breast cancer."
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"Moreover, we show that Usp8 interacts with ErbB2 and is tyrosine phosphorylated in a ErbB2- and Src kinase-dependent manner, although its tyrosine phosphorylation is to a lesser extent than in the cas[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The IP and IB analysis found that HER2 and USP8 bound each other, especially N-HER2 (Fig. xref ), and USP8 mainly inhibited N-HER2 ubiquitination (Fig. xref )."
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"When MALAT1 was overexpressed, the interaction between HER2 and USP8 was increased (Fig. xref )."
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"When MALAT1 was overexpressed, the interaction between HER2 and USP8 was increased (Fig. 3G)."
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