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• W2618291208 endingPage "170042" @default.
• W2618291208 startingPage "170042" @default.
• W2618291208 abstract "Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1), an FCP/SCP phosphatase family member, was identified as the first proteasome phosphatase. UBLCP1 binds to proteasome subunit Rpn1 and dephosphorylates the proteasome in vitro However, it is still unclear which proteasome subunit(s) are the bona fide substrate(s) of UBLCP1 and the precise mechanism for proteasome regulation remains elusive. Here, we show that UBLCP1 selectively binds to the 19S regulatory particle (RP) through its interaction with Rpn1, but not the 20S core particle (CP) or the 26S proteasome holoenzyme. In the RP, UBLCP1 dephosphorylates the subunit Rpt1, impairs its ATPase activity, and consequently disrupts the 26S proteasome assembly, yet it has no effects on the RP assembly from precursor complexes. The Rpn1-binding and phosphatase activities of UBLCP1 are essential for its function on Rpt1 dephosphorylation and proteasome activity both in vivo and in vitro Our study establishes the essential role of the UBLCP1/Rpn1/Rpt1 complex in regulating proteasome assembly." @default.
• W2618291208 created "2017-06-05" @default.
• W2618291208 creator A5022231767 @default.
• W2618291208 creator A5051676178 @default.
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• W2618291208 creator A5065371838 @default.
• W2618291208 creator A5068139112 @default.
• W2618291208 date "2017-05-01" @default.
• W2618291208 modified "2023-10-18" @default.
• W2618291208 title "Phosphatase UBLCP1 controls proteasome assembly" @default.
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• W2618291208 doi "https://doi.org/10.1098/rsob.170042" @default.
• W2618291208 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5451543" @default.
• W2618291208 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28539385" @default.
• W2618291208 hasPublicationYear "2017" @default.
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