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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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Density Gradient Ultracentrifugation for Investigating Endocytic Recycling in Mammalian Cells
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Published on: June 30, 2021

RNF13 regulates the endolysosomal pathway through interaction with the small GTPase Arl8B.

Audrey M Sénécal1,2,3, Valérie C Cabana1,2,3, Antoine Y Bouchard1,2,3

  • 1Department of Chemistry, Université du Québec à Montréal, Canada.

The FEBS Journal
|May 28, 2026
PubMed
Summary
This summary is machine-generated.

The E3 ubiquitin ligase RNF13 regulates endolysosomal dynamics by binding to the GTPase Arl8B, influencing lysosome positioning and epidermal growth factor receptor (EGFR) trafficking to degradation pathways.

Keywords:
Arl8BRNF13endolysosomal traffickinglysosome positioningprotein–protein interaction

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Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The endolysosomal system is crucial for cellular waste disposal and recycling.
  • Proper regulation of endosome maturation and positioning is vital for lysosomal function and receptor turnover.
  • The small GTPase Arl8B plays a role in endolysosomal positioning and trafficking.

Purpose of the Study:

  • To investigate the role of the E3 ubiquitin ligase RNF13 in endolysosomal dynamics.
  • To identify potential interactions between RNF13 and components of the endolysosomal system, specifically Arl8B.
  • To elucidate the functional consequences of the RNF13-Arl8B interaction on lysosomal organization and cargo trafficking.

Main Methods:

  • Predictive structural modeling to predict binding interfaces.
  • Co-immunoprecipitation assays to confirm RNF13-Arl8B interaction.
  • Cell-based assays to assess the impact of disrupting RNF13-Arl8B binding on lysosomal localization and EGFR trafficking.

Main Results:

  • RNF13 directly binds to Arl8B, with a preference for the GDP-bound state.
  • Disruption of RNF13-Arl8B interaction alters Arl8B localization and causes lysosome redistribution to the cell periphery.
  • Perturbing the interaction selectively delays epidermal growth factor receptor (EGFR) degradation without affecting general endocytosis.
  • RNF13 influences Arl8B-dependent trafficking complexes and lysosomal organization.

Conclusions:

  • RNF13 acts as a novel regulator of lysosomal positioning and endolysosomal cargo transport.
  • The interaction between RNF13 and Arl8B provides a new regulatory mechanism for trafficking pathways.
  • RNF13 highlights a regulatory node influencing cargo progression through degradative pathways via Arl8B binding and ubiquitination.