Ubiquitination within the membrane-proximal ezrin-radixin-moesin (ERM)-binding region of the L1 cell adhesion molecule

The dynamic turnover of the L1 cell adhesion molecule to and from the plasma membrane that is mediated through exo-and endocytic trafficking is central to axon outgrowth. Although the ubiquitination of L1 in response to incubation with an L1 antibody that mimics L1-L1 homophilic binding has been pre...

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Bibliographic Details
Published inCommunicative & integrative biology Vol. 6; no. 4; p. e24750
Main Author Aikawa, Yoshikatsu
Format Journal Article
LanguageEnglish
Published United States Landes Bioscience 30.07.2013
Subjects
Short Communication
cell adhesion molecule
endocytosis
ezrin
L1
ubiquitin
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Summary:The dynamic turnover of the L1 cell adhesion molecule to and from the plasma membrane that is mediated through exo-and endocytic trafficking is central to axon outgrowth. Although the ubiquitination of L1 in response to incubation with an L1 antibody that mimics L1-L1 homophilic binding has been previously shown, the endocytic trafficking pathway of the ubiquitinated L1 destined for degradation is yet unclear. I have recently shown that the ubiquitinated L1 is endocytosed by Rabex-5, which is an ubiquitin-binding protein and guanine nucleotide exchange factor for Rab5, into early endosomes from the plasma membrane. Here, I speculate on the putative ubiquitination site within the membrane-proximal ezrin-binding motif in the cytoplasmic domain of L1 and discuss the regulatory role of this motif in the competition between ubiquitination and the binding of ezrin prior to L1 internalization.
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ISSN:1942-0889
1942-0889
DOI:10.4161/cib.24750