L1CAM ubiquitination facilitates its lysosomal degradation
L1CAM ubiquitination facilitates its lysosomal degradation
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L1CAM 泛素化促进其溶酶体降解
DOI：
10.1016/j.febslet.2010.10.011
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发表时间：
2010
期刊：
影响因子：
3.5
通讯作者：
S. Diestel
中科院分区：
文献类型：
--
作者：
Michael K. E. Schäfer;B. Schmitz;S. Diestel
细胞黏附分子L1参与发育和成人神经系统的几个过程。L1在细胞内的运输对细胞迁移、突起生长和黏附非常重要。我们在这里证明了L1在质膜和早期内吞体内是泛素化的。单一泛素化通过促进L1溶酶体的降解来调节L1的细胞内转运。我们认为L1‘S泛素化可能是一种额外的机制来控制其在细胞表面的重新出现，从而影响轴突生长和细胞黏附等过程。
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.