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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog
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Spotlight on USP4: Structure, Function, and Regulation.

Binbin Hu1, Dingyue Zhang1, Kejia Zhao2

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Summary
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Ubiquitin-specific protease 4 (USP4) deubiquitinating enzyme is crucial for protein balance. Aberrant USP4 activity links to cancer, necessitating therapeutic targeting.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Deubiquitinating enzymes (DUBs) regulate protein homeostasis by cleaving ubiquitin.
  • USP4, a cysteine protease DUB, removes ubiquitin chains from target proteins.
  • USP4's structure includes DUSP-UBL and UBL-insert catalytic domains, similar to USP11 and USP15.

Purpose of the Study:

  • To comprehensively review the structure, biological functions, and pathological roles of USP4.
  • To summarize the cellular regulation mechanisms of USP4.
  • To highlight the therapeutic potential of targeting USP4 in diseases, particularly cancer.

Main Methods:

  • Literature review of existing research on USP4.
  • Analysis of USP4's structural and functional domains.
  • Examination of USP4's involvement in cellular processes and disease.

Main Results:

  • USP4 is vital for cellular processes and tightly regulated.
  • Dysregulated USP4 expression or activity is implicated in various pathologies, especially cancers.
  • USP4's paralogs USP11 and USP15 share similar domain organization.

Conclusions:

  • USP4 plays a critical role in balancing protein synthesis and degradation.
  • Aberrant USP4 activity is a significant factor in cancer progression.
  • Further research into USP4 is crucial for developing targeted therapeutic strategies.