L1CAM ubiquitination facilitates its lysosomal degradation |
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| Authors: | Schäfer Michael K E Schmitz Brigitte Diestel Simone |
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| Institution: | a Institute of Anatomy and Cell Biology, Center for Neurosciences, University of Freiburg, 79104 Freiburg, Germany
b Institute of Animal Sciences, Department of Biochemistry, University of Bonn, 53115 Bonn, Germany |
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| 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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| Keywords: | Ubi ubiquitin IP immunoprecipitation IB immunoblot wt wild type HA hemagglutinin DUB de-ubiquitinating enzyme |
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