Structure/function relationships of axon-associated adhesion receptors of the immunoglobulin superfamily.
Evidence is accumulating that axonal members of the Ig superfamily (IgSF) interact in a complex manner with other axonal Ig-like proteins and with proteins of the extracellular matrix. Studies investigating the structure/function relationships of these proteins have highlighted the importance of Ig-like domains near the amino terminus (N-proximal) as both necessary and sufficient for homophilic and heterophilic binding. Although efforts have been made in the past year to correlate the structure and neurite-outgrowth-promoting ability of axonal IgSF members, this work is still at an early stage.
Brümmendorf
T
T
Max-Planck-Institut für Entwicklungsbiologie,Tübingen, Germany. brue@mpib-tuebingen.mpg.de
Rathjen
F G
FG
D000818:Animals; D001369:Axons / Q000502:physiology*; D001665:Binding Sites; D002448:Cell Adhesion; D005109:Extracellular Matrix / Q000502:physiology; D006801:Humans; D007136:Immunoglobulins / Q000502:physiology*; D016023:Integrins / Q000502:physiology*; D019006:Neural Cell Adhesion Molecules / Q000502:physiology*; D016501:Neurites / Q000502:physiology; D009474:Neurons / Q000166:cytology / Q000502:physiology*
D007136:Immunoglobulins; D016023:Integrins; D019006:Neural Cell Adhesion Molecules