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Related Concept Videos

Enzymes02:34

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The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
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Updated: Feb 3, 2026

A Scalable, Cell-Based Method for the Functional Assessment of Ube3a Variants
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A Scalable, Cell-Based Method for the Functional Assessment of Ube3a Variants

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Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex.

Carolin Sailer1, Fabian Offensperger1, Alexandra Julier1

  • 1Department of Biology, University of Konstanz, Universitätsstrasse 10, 78457, Konstanz, Germany.

Nature Communications
|October 27, 2018
PubMed
Summary
This summary is machine-generated.

Deregulation of ubiquitin ligase E6AP contributes to cervical cancer by targeting the tumor suppressor p53. This study reveals how E6 oncoprotein activates E6AP, structurally enabling p53 degradation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Deregulation of E6AP ubiquitin ligase is linked to human diseases, including cervical cancer.
  • The E6 oncoprotein of human papillomaviruses complexes with E6AP to degrade the tumor suppressor p53, promoting carcinogenesis.
  • The mechanism by which E6 activates E6AP and the structural assembly of the E6AP-E6-p53 complex remain largely unelucidated.

Purpose of the Study:

  • To investigate the structural and functional interplay between E6AP, E6 oncoprotein, and p53.
  • To elucidate the mechanism of E6-mediated activation of E6AP's ubiquitin ligase activity.
  • To gain structural insights into the E6AP-E6-p53 enzyme-substrate complex assembly.

Main Methods:

  • Development and application of crosslinking mass spectrometry-based approaches.
  • Analysis of the E6AP-E6-p53 complex dynamics.
  • Structural and functional characterization of enzyme-substrate interactions.

Main Results:

  • Binding of E6 induces conformational changes in E6AP.
  • E6 positions both itself and p53 near E6AP's catalytic center.
  • Structural and functional insights into the E6AP-E6-p53 complex dynamics were obtained.

Conclusions:

  • E6 activates E6AP's ubiquitin ligase activity through conformational rearrangements.
  • The study elucidates how E6 facilitates ubiquitin transfer from E6AP to p53.
  • Provides a structural basis for E6AP's role in p53 degradation and carcinogenesis.