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Updated: Jun 8, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
Published on: January 2, 2026
L1CAM ubiquitination facilitates its lysosomal degradation
Michael K E Schäfer1, Brigitte Schmitz, Simone Diestel
1Institute of Anatomy and Cell Biology, Center for Neurosciences, University of Freiburg, Freiburg, Germany.
Abstract:
The cell adhesion molecule L1 is implicated in several processes in the developing and adult nervous system. Intracellular trafficking of L1 is important for cell migration, neurite growth and adhesion. We demonstrate here that L1 is ubiquitinated at the plasma membrane and in early endosomes. Mono-ubiquitination regulates L1 intracellular trafficking by enhancing its lysosomal degradation. We propose that L1's ubiquitination might be an additional mechanism to control its re-appearance at the cell surface thereby influencing processes like neurite growth and cell adhesion.
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