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Publication : L1CAM ubiquitination facilitates its lysosomal degradation.

First Author  Schäfer MK Year  2010
Journal  FEBS Lett Volume  584
Issue  21 Pages  4475-80
PubMed ID  20940017 Mgi Jnum  J:165502
Mgi Id  MGI:4837578 Doi  10.1016/j.febslet.2010.10.011
Citation  Schafer MK, et al. (2010) L1CAM ubiquitination facilitates its lysosomal degradation. FEBS Lett 584(21):4475-80
abstractText  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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