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L1CAM ubiquitination facilitates its lysosomal degradation
Author(s) -
Schäfer Michael K.E.,
Schmitz Brigitte,
Diestel Simone
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.10.011
Subject(s) - endosome , microbiology and biotechnology , ubiquitin , intracellular , neurite , cell adhesion , adhesion , l1 , chemistry , neural cell adhesion molecule , lysosome , cell adhesion molecule , endocytosis , cell , biology , biochemistry , in vitro , enzyme , organic chemistry , gene
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.