Cell Adhesion Molecules and Ubiquitination—Functions and Significance

Biology

Mirka Homrich²  Ingo Gotthard²  Hilke Wobst²  Simone Diestel¹ 

[1] Department of Human Metabolomics, Institute of Nutrition and Food Sciences, University of Bonn, Katzenburgweg 9a, Bonn 53115, Germany

关键词: immunoglobulin superfamily;    cell adhesion molecules;    posttranslational modification;    ubiquitination;    endocytosis;    intracellular trafficking;   

DOI  :  10.3390/biology5010001

来源: mdpi

【 摘 要 】

Cell adhesion molecules of the immunoglobulin (Ig) superfamily represent the biggest group of cell adhesion molecules. They have been analyzed since approximately 40 years ago and most of them have been shown to play a role in tumor progression and in the nervous system. All members of the Ig superfamily are intensively posttranslationally modified. However, many aspects of their cellular functions are not yet known. Since a few years ago it is known that some of the Ig superfamily members are modified by ubiquitin. Ubiquitination has classically been described as a proteasomal degradation signal but during the last years it became obvious that it can regulate many other processes including internalization of cell surface molecules and lysosomal sorting. The purpose of this review is to summarize the current knowledge about the ubiquitination of cell adhesion molecules of the Ig superfamily and to discuss its potential physiological roles in tumorigenesis and in the nervous system.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.