IndraLab

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FZR1 binds USP8. 31 / 31
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"Given that USP8 contains a ubiquitin C-terminal hydrolase (UCH) domain at the C terminus and a dimerization domain at the N terminus ( xref ), we investigated which of these domains might be involved in the USP8-Fzr interaction."
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"Hsp70 promotes the USP8-Fzr interaction, thereby maintaining Fzr stability via deubiquitination to regulate endoreplication."
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"Second, to determine whether USP8 interacts with Fzr in vivo, we co-overexpressed HA-tagged USP8 and Flag-tagged Fzr in Bombyx BmE cells and Drosophila S2 cells and then conducted coimmunoprecipitation (co-IP) experiments with specific antibodies."
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"Similarly, further co-IP experiments confirmed the interaction between endogenous USP8 and Fzr in cultured BmE cells and S2 cells ( xref and fig."
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"Third, glutathione S -transferase (GST) pull-down assays revealed that bacterially purified recombinant Trx-His–tagged USP8 interacted with recombinant GST-tagged Fzr in vitro (fig."
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"Together, our data suggest that Hsp70 mediates proper folding of Fzr, thereby promoting the interaction of Fzr with USP8."
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"Collectively, these data demonstrate that USP8 physically interacts with Fzr."
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"Furthermore, to determine which of WD40 domains in Fzr proteins might be involved in the USP8-Fzr interaction, we generated a series of constructs for overexpressing truncated Fzr with the deletion of single WD40 domain and then performed co-IP assays in cultured cells."
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"Collectively, our findings reveal that Hsp70 regulates endoreplication by promoting the USP8-Fzr interaction and subsequently modulating Fzr deubiquitination and stabilization."
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"Mechanistically, USP8 interacts with Fzr to deubiquitinate and stabilize Fzr."
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"These results were consistent with the AlphaFold 3–based prediction, further confirming that different WD40 domains of Fzr proteins mediate the interaction of Fzr with USP8 in Bombyx and Drosophila ."
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"Hsp70 promotes the interaction between USP8 and Fzr."
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"The molecular chaperone Hsp70 promotes the interaction of Fzr with USP8 by mediating Fzr folding, thereby participating in endoreplication progression."
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"Since the interaction between USP8 and Fzr indicated by in vitro GST pull-down assays (fig."
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"We next investigated whether Hsp70 is associated with the USP8-Fzr interaction."
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"S9, E and F) was relatively slight compared to that shown by in vivo co-IP assays ( xref ), we speculated that other cofactors may modulate the USP8-Fzr interaction."
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"Co-IP experiments showed that Hsp70 overexpression promoted the interaction between exogenously overexpressed USP8 and Fzr in BmE cells and S2 cells ( xref )."
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"Since proper folding of proteins generally devotes to their interactions with other partners ( xref ), like the WD40 protein Bub3 ( xref ), we thus suggest that the interaction of Hsp70 with Fzr facilitates proper folding of Fzr, thereby enhancing the interaction of Fzr with USP8 to promote Fzr deubiquitination and stabilization during endoreplication."
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"Similarly, GST pull-down assays confirmed that Hsp70 supplementation enhanced the USP8-Fzr interaction ( xref )."
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"Furthermore, we examined the change of the USP8-Fzr interaction following treatment for 2 hours with PES as a Hsp70 activity inhibitor."
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"Moreover, the molecular chaperone heat shock protein 70 (Hsp70) mediated proper folding of Fzr and increased the interaction between Fzr and USP8, thereby promoting the deubiquitination and stabilization of Fzr."
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"S8), indicating a potential interaction between USP8 and Fzr."
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"Similarly, further co-IP experiments confirmed the interaction between endogenous USP8 and Fzr in cultured BmE cells and S2 cells (Fig. 3C and fig."
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"Hsp70 promotes the interaction between USP8 and Fzr."
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"The results showed that PES treatment attenuated the interaction between endogenous USP8 and Fzr in ex vivo–cultured PSGs and salivary glands ( xref ) as well as in BmE cells and S2 cells ( xref )."
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"USP8 physically interacts with Fzr."
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"The results showed that PES treatment attenuated the interaction between endogenous USP8 and Fzr in ex vivo–cultured PSGs and salivary glands (Fig. 5, E and F) as well as in BmE cells and S2 cells (Fig. 5, G and H)."
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"Given that Fzr proteins from Bombyx and Drosophila contain different numbers of WD40 domains that mediate protein-protein interaction, we thus investigated whether USP8 interacts with Fzr."
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"Moreover, we investigate possible mechanism by which Hsp70 facilitates the USP8-Fzr interaction."
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"S8), indicating a potential interaction between USP8 and Fzr."
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"Moreover, the molecular chaperone heat shock protein 70 (Hsp70) mediated proper folding of Fzr and increased the interaction between Fzr and USP8, thereby promoting the deubiquitination and stabilization of Fzr."
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