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Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Phosphatase UBLCP1 controls proteasome assembly.

Shuangwu Sun1, Sisi Liu1, Zhengmao Zhang2,3

  • 1Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang, People's Republic of China.

Open Biology
|May 26, 2017
PubMed
Summary
This summary is machine-generated.

Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1) regulates proteasome assembly by dephosphorylating Rpt1. This interaction, mediated by Rpn1, is crucial for proteasome function.

Keywords:
CTD phosphataseUBLCP1phosphorylationproteasome

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1) is a proteasome phosphatase.
  • Its precise substrates and regulatory mechanisms within the proteasome remain unclear.

Purpose of the Study:

  • To elucidate the specific proteasome subunit targeted by UBLCP1.
  • To define the role of UBLCP1 in proteasome regulation and assembly.

Main Methods:

  • In vitro binding assays to determine UBLCP1 interaction sites within the proteasome.
  • In vitro and in vivo assays to assess the phosphatase activity of UBLCP1 on proteasome subunits.
  • Analysis of proteasome assembly and ATPase activity.

Main Results:

  • UBLCP1 selectively binds to the 19S regulatory particle (RP) via Rpn1.
  • UBLCP1 dephosphorylates the Rpt1 subunit, impairing its ATPase activity.
  • This dephosphorylation disrupts 26S proteasome holoenzyme assembly but not RP precursor assembly.
  • Both Rpn1 binding and phosphatase activity of UBLCP1 are essential for its function.

Conclusions:

  • UBLCP1 acts as a key regulator of proteasome assembly through the UBLCP1/Rpn1/Rpt1 complex.
  • UBLCP1's phosphatase activity on Rpt1 is critical for controlling proteasome function.