IndraLab

Statements

USP19 binds HSP90. 12 / 12
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"It is the first DUB reported to be regulated by heat shock protein, Hsp90, which binds with the catalytic domain of USP19 and promotes its substrate association."
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"Biochemical study showed that USP19 binds to two major heat shock proteins HSC70 and HSP90 in cells, suggesting a possible role in PQC (Lee et al., 2014)."
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"The interaction of USP19 with HSP90 accelerates the aggregation of HTT by modulating the protein level of HTT, confirming that the effect of USP19 decreases when the interaction between HTT and HSP90 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Indeed, an interaction of USP19 with Hsp90 has been described ( He et al., 2016; Lee et al., 2014 )."
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"Collectively, the cytoplasmic USP19 associates with HSP90 potentially forming a dynamic complex in cells, which may function in quality control for the polyQ-expanded proteins."
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"Both forms of USP19 specifically interact with HSP90 through their N-terminal CS domains and then associate with CHIP via HSP90."
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"The regulatory function of USP19 was recently confirmed in a study demonstrating that USP19 interacts directly with chaperone Hsp90 and upregulates the aggregation of poly-Q containing the proteins Ataxin-3 and Huntingtin, which causes spinocerebellar ataxia type-3 and Huntington’s disease, respectively [ xref ]."
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"Thus, HSP90 interacts with Htt-N90 on the N-terminal amphipathic alpha-helix, and then recruits USP19 to modulate the protein level and aggregation of Htt-N90."
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"HSP90 interacts with the N-terminus of HTT and recruits USP19, thereby affecting the expression level and aggregation of HTT ( He et al., 2017 )."
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"However, when the TM domain was removed, the C-terminal (CT) fragment of USP19 could now bind Hsp90 almost as efficiently as full-length WT USP19."
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"This suggests that the Hsp90–Usp19 complex can simultaneously mobilize two dcTPR proteins via their MEEVD C termini."
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"This suggests that the Hsp90–Usp19 complex can simultaneously mobilize two dcTPR proteins via their MEEVD C termini."
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